Annexin-Phospholipid Interactions. Functional Implications

Lizarbe, María; Barrasa, Juan; Olmo, Nieves; Gavilanes, Francisco; Turnay, Javier

doi:10.3390/ijms14022652

Cited by 234S100 Proteins and AnnexinsLipid Membrane Structure and BehaviorProtein Interaction Studies and Fluorescence Analysis

Annexin-Phospholipid Interactions. Functional Implications

Open access

Lizarbe, María, Barrasa, Juan, Olmo, Nieves, Gavilanes, Francisco, Turnay, Javier·2013·International Journal of Molecular Sciences

DOI 10.3390/ijms14022652PMC PMC3588008

Open this paper in CoChat — free account Open PDF

Abstract

Annexins constitute an evolutionary conserved multigene protein superfamily characterized by their ability to interact with biological membranes in a calcium dependent manner. They are expressed by all living organisms with the exception of certain unicellular organisms. The vertebrate annexin core is composed of four (eight in annexin A6) homologous domains of around 70 amino acids, with the overall shape of a slightly bent ring surrounding a central hydrophilic pore. Calcium- and phospholipid-binding sites are located on the convex side while the N-terminus links domains I and IV on the concave side. The N-terminus region shows great variability in length and amino acid sequence and it greatly influences protein stability and specific functions of annexins. These proteins interact mainly with acidic phospholipids, such as phosphatidylserine, but differences are found regarding their affinity for lipids and calcium requirements for the interaction. Annexins are involved in a wide range of intra- and extracellular biological processes in vitro, most of them directly related with the conserved ability to bind to phospholipid bilayers: membrane trafficking, membrane-cytoskeleton anchorage, ion channel activity and regulation, as well as antiinflammatory and anticoagulant activities. However, the in vivo physiological functions of annexins are just beginning to be established.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.3390/ijms14022652

Cites

171 of 171 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Binding of annexins to acidic phospholipids or other interaction partners can be modulated by Ca2+ ions and influences diverse cellular processes such as vesicle trafficking, signaling, and membrane-cytoskeleton interactions.
“The binding of annexins to acidic phospholipids or other interaction partners can be modulated by the presence of Ca2+ ions and influences diverse cellular processes such as vesicle trafficking, signaling, and membrane-cytoskeleton interactions (2).”
From Comparative Cell Biology and Evolution of Annexins in Diplomonads (2016) · cites this paper as [2]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

MOLMOL: A program for display and analysis of macromolecular structures
Koradi, R., Billeter, M., & Kurt Wüthrich, A. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00009-4 · Cited by 7,163 · see citing works
Apoptosis: controlled demolition at the cellular level
Taylor, R. C., Cullen, S. P., & Martin, S. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2312 · Cited by 2,617 · see citing works
Annexins: From Structure to Function
Gerke, V., & Moss, S. E. (2002) · Physiological Reviews · doi:10.1152/physrev.00030.2001 · Cited by 2,029 · see citing works
Annexins: linking Ca2+ signalling to membrane dynamics
Gerke, V., Creutz, C. E., & Moss, S. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1661 · Cited by 1,412 · see citing works
Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins
Raynal, P., & Pollard, H. B. (1994) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(94)90019-1 · Cited by 1,115 · see citing works
The Ceramide-centric Universe of Lipid-mediated Cell Regulation: Stress Encounters of the Lipid Kind
Hannun, Y. A., & Obeid, L. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.r200008200 · Cited by 910 · see citing works
The mitochondrial pathways of apoptosis
Estaquier, J., Vallette, F., Vayssiere, J.-L., & Mignotte, B. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2869-1_7 · Cited by 637 · see citing works
Sphingolipid-modulated Exosome Secretion Promotes Clearance of Amyloid-β by Microglia
Yuyama, K., Sun, H., Mitsutake, S., & Igarashi, Y. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.324616 · Cited by 591 · see citing works
Find-me and eat-me signals in apoptotic cell clearance: progress and conundrums
Ravichandran, K. S. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20101157 · Cited by 547 · see citing works
In vivo detection and imaging of phosphatidylserine expression during programmed cell death
Blankenberg, F. G., Katsikis, P. D., Tait, J. F., Davis, R. E., Naumovski, L., Ohtsuki, K., Kopiwoda, S. Y., Abrams, M. J., Darkes, M. C., Robbins, R. C., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6349 · Cited by 536 · see citing works
Annexin I Is an Endogenous Ligand that Mediates Apoptotic Cell Engulfment
Arur, S., Uche, U. E., Rezaul, K., Fong, M., Scranton, V., Cowan, A. E., Mohler, W., & Han, D. K. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00090-x · Cited by 434 · see citing works
Clearance of apoptotic cells by phagocytes
Erwig, L.-P., & Henson, P. M. (2008) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402184 · Cited by 422 · see citing works
A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A
van der Goot, F. G., González‐Mañas, J. M., Lakey, J. H., & Pattus, F. (1991) · Nature · doi:10.1038/354408a0 · Cited by 418 · see citing works
The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes.
Huber, R., Römisch, J., & PÂQUES, E. P. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07605.x · Cited by 410 · see citing works
Dysferlin Interacts with Annexins A1 and A2 and Mediates Sarcolemmal Wound-healing
Lennon, N. J., Kho, A. T., Bacskai, B. J., Perlmutter, S. L., Hyman, B. T., & Brown, R. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307247200 · Cited by 407 · see citing works
Aminophospholipid Asymmetry: A Matter of Life and Death
Balasubramanian, K., & Schroit, A. J. (2003) · Annual Review of Physiology · doi:10.1146/annurev.physiol.65.092101.142459 · Cited by 396 · see citing works
Annexin II regulates fibrin homeostasis and neoangiogenesis in vivo
Qi, L., Jacovina, A. T., Deora, A. B., Febbraio, M., Simantov, R., Silverstein, R. L., Hempstead, B. L., Mark, W. H., & Hajjar, K. A. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19684 · Cited by 381 · see citing works
EGF stimulates annexin 1‐dependent inward vesiculation in a multivesicular endosome subpopulation
White, I. J., Bailey, L. M., Aghakhani, M. R., Moss, S. E., & Futter, C. E. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600759 · Cited by 367 · see citing works
Past, present, and future of annexin A5: from protein discovery to clinical applications.
Boersma, H. H., Kietselaer, B., Stolk, L. M., Bennaghmouch, A., Hofstra, L., Narula, J., Heidendal, G. A. K., & Reutelingsperger, C. P. M. (2005) · PubMed · Cited by 333 · see citing works
Ca2+-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V
Swairjo, M. A., Concha, N. O., Kaetzel, M. A., Dedman, J. R., & Seaton, B. A. (1995) · Nature Structural & Molecular Biology · doi:10.1038/nsb1195-968 · Cited by 313 · see citing works
Characterization of Ca2+-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins
Blackwood, R. A., & Ernst, J. (1990) · Biochemical Journal · doi:10.1042/bj2660195 · Cited by 292 · see citing works
Annexin-A5 assembled into two-dimensional arrays promotes cell membrane repair
Bouter, A., Gounou, C., Bérat, R., Tan, S., Gallois, B., Granier, T., d’Estaintot, B. L., Pöschl, E., Brachvogel, B., & Brisson, A. R. (2011) · Nature Communications · doi:10.1038/ncomms1270 · Cited by 283 · see citing works
Identifying mRNA, MicroRNA and Protein Profiles of Melanoma Exosomes
Xiao, D., Ohlendorf, J. M., Chen, Y., Taylor, D. D., Rai, S. N., Waigel, S. J., Zacharias, W., Hao, H., & McMasters, K. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046874 · Cited by 277 · see citing works
Annexins in Cell Membrane Dynamics
Babiychuk, E. B., & Draeger, A. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.5.1113 · Cited by 266 · see citing works
Transbilayer (flip‐flop) lipid motion and lipid scrambling in membranes
Contreras, F. ‐., Sánchez‐Magraner, L., Alonso, A., & Goñi, F. M. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.12.049 · Cited by 264 · see citing works
Annexin–Actin Interactions
Hayes, M. J., Rescher, U., Gerke, V., & Moss, S. E. (2004) · Traffic · doi:10.1111/j.1600-0854.2004.00210.x · Cited by 257 · see citing works
The calcium binding sites in human annexin V by crystal structure analysis at 2.0 A resolution Implications for membrane binding and calcium channel activity
Huber, R., Schneider, M., Mayr, I., Römisch, J., & Pâques, E.-P. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)81428-q · Cited by 244 · see citing works
Requirement for Annexin A1 in Plasma Membrane Repair
McNeil, A. K., Rescher, U., Gerke, V., & McNeil, P. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606406200 · Cited by 232 · see citing works
Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C.
Chung, C. Y., & Erickson, H. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.2.539 · Cited by 232 · see citing works
Extracellular annexin A5: Functions of phosphatidylserine-binding and two-dimensional crystallization
van Genderen, H., Kenis, H., Hofstra, L., Narula, J., & Reutelingsperger, C. P. M. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.01.030 · Cited by 229 · see citing works
Detachment of Breast Tumor Cells Induces Rapid Secretion of Exosomes Which Subsequently Mediate Cellular Adhesion and Spreading
Koumangoye, R. B., Sakwe, A. M., Goodwin, J. S., Patel, T., & Ochieng, J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024234 · Cited by 227 · see citing works
Plasma membrane repair and cellular damage control: The annexin survival kit
Draeger, A., Monastyrskaya, K., & Babiychuk, E. B. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2010.12.027 · Cited by 217 · see citing works
Domain coupling in asymmetric lipid bilayers
Kiessling, V., Wan, C., & Tamm, L. K. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.09.003 · Cited by 217 · see citing works
Annexin Structure and Membrane Interactions: A Molecular Perspective
Swairjo, M. A., & Seaton, B. A. (1994) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.bb.23.060194.001205 · Cited by 213 · see citing works
Beyond annexin V: fluorescence response of cellular membranes to apoptosis
Demchenko, A. P. (2012) · Cytotechnology · doi:10.1007/s10616-012-9481-y · Cited by 206 · see citing works
A novel calcium‐dependent proapoptotic effect of annexin 1 on human neutrophils
Solito, E., Kamal, A. M., Russo‐Marie, F., Buckingham, J. C., Marullo, S., & Perretti, M. (2003) · The FASEB Journal · doi:10.1096/fj.02-0941fje · Cited by 199 · see citing works
Annexin‐A1: a pivotal regulator of the innate and adaptive immune systems
D’Acquisto, F., Perretti, M., & Flower, R. J. (2008) · British Journal of Pharmacology · doi:10.1038/bjp.2008.252 · Cited by 194 · see citing works
Annexin II Binds to Capsid Protein VP1 of Enterovirus 71 and Enhances Viral Infectivity
Yang, S.-L., Chou, Y.-T., Wu, C.-N., & Ho, M. (2011) · Journal of Virology · doi:10.1128/jvi.00297-11 · Cited by 176 · see citing works
Annexin A2-Dependent Polymerization of Actin Mediates Endosome Biogenesis
Morel, É., Parton, R. G., & Grüenberg, J. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.01.007 · Cited by 174 · see citing works
Three-dimensional Structure of Membrane-bound Annexin V
Voges, D., Berendes, R., Bürger, A., Demange, P., Baumeister, W. P., & Huber, R. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1281 · Cited by 173 · see citing works
Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes
Rescher, U., Ruhe, D., Ludwig, C., Zobiack, N., & Gerke, V. (2004) · Journal of Cell Science · doi:10.1242/jcs.01208 · Cited by 169 · see citing works
Properties of cytotoxic peptide-formed ion channels
Kourie, J. I., & Shorthouse, A. (2000) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2000.278.6.c1063 · Cited by 158 · see citing works
Annexin XIIIb: a novel epithelial specific annexin is implicated in vesicular traffic to the apical plasma membrane.
Fiedler, K., Lafont, F., Parton, R. G., & Simons, K. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.128.6.1043 · Cited by 151 · see citing works
Annexins and Endocytosis
Futter, C. E., & White, I. J. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00590.x · Cited by 150 · see citing works
Evolutionary adaptation of plant annexins has diversified their molecular structures, interactions and functional roles
Clark, G. B., Morgan, R. O., Fernandez, M., & Roux, S. J. (2012) · New Phytologist · doi:10.1111/j.1469-8137.2012.04308.x · Cited by 150 · see citing works
Annexins — Modulators of EGF receptor signalling and trafficking
Grewal, T., & Enrich, C. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.01.031 · Cited by 146 · see citing works
Annexin 2 Promotes the Formation of Lipid Microdomains Required for Calcium-regulated Exocytosis of Dense-Core Vesicles
Chasserot‐Golaz, S., Vitale, N., Umbrecht-Jenck, E., KNIGHT, D. E., Gerke, V., & Bader, M. F. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-07-0627 · Cited by 142 · see citing works
The annexins: spatial and temporal coordination of signaling events during cellular stress
Monastyrskaya, K., Babiychuk, E. B., & Draeger, A. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0027-1 · Cited by 139 · see citing works
A Calcium-driven Conformational Switch of the N-terminal and Core Domains of Annexin A1
Rosengarth, A., & Luecke, H. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00027-5 · Cited by 139 · see citing works
New reagents for phosphatidylserine recognition and detection of apoptosis
Hanshaw, R. G., & Smith, B. D. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.04.071 · Cited by 133 · see citing works
X-ray structure of full-length annexin 1 and implications for membrane aggregation11Edited by D. Rees
Rosengarth, A., Gerke, V., & Luecke, H. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4423 · Cited by 131 · see citing works
Role of Annexin A2 in the Production of Infectious Hepatitis C Virus Particles
Backes, P., Quinkert, D., Reiss, S., Binder, M., Zayas, M., Rescher, U., Gerke, V., Bartenschlager, R. F. W., & Lohmann, V. (2010) · Journal of Virology · doi:10.1128/jvi.02343-09 · Cited by 131 · see citing works
Crystal structure of the annexin XII hexamer and implications for bilayer insertion
Luecke, H., Chang, B. T., Mailliard, W. S., Schlaepfer, D. D., & Haigler, H. T. (1995) · Nature · doi:10.1038/378512a0 · Cited by 127 · see citing works
The role of the annexin A2 heterotetramer in vascular fibrinolysis
Madureira, P. A., Surette, A. P., Phipps, K. D., Taboski, M. A. S., Miller, V. A., & Waisman, D. M. (2011) · Blood · doi:10.1182/blood-2011-06-334672 · Cited by 123 · see citing works
Structural and functional characterization of endonexin II, a calcium- and phospholipid-binding protein.
Schlaepfer, D. D., Mehlman, T., Burgess, W. H., & Haigler, H. T. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.17.6078 · Cited by 121 · see citing works
The Crystal Structure of a New High-calcium Form of Annexin V
Sopková, J., Renouard, M., & Lewit‐Bentley, A. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1627 · Cited by 119 · see citing works
HAb18G/CD147 promotes cell motility by regulating annexin II-activated RhoA and Rac1 signaling pathways in hepatocellular carcinoma cells
Zhao, P., Zhang, W., Wang, S., Yu, X., Tang, J., Huang, W., Li, Y., Cui, H., Guo, Y., Tavernier, J. H., et al. (2010) · Hepatology · doi:10.1002/hep.24592 · Cited by 116 · see citing works
Biochemical characterization of detergent-resistant membranes: a systematic approach
Babiychuk, E. B., & Draeger, A. (2006) · Biochemical Journal · doi:10.1042/bj20060056 · Cited by 112 · see citing works
Annexin A6‐Induced Alterations in Cholesterol Transport and Caveolin Export from the Golgi Complex
Cubells, L., de Muga, S. V., Tebar, F., Wood, P., Evans, R., Ingelmo‐Torres, M., Calvo, M., Gaus, K., Pol, A., Grewal, T., et al. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00640.x · Cited by 112 · see citing works
The Structure of Recombinant Human Annexin VI in Crystals and Membrane-bound
Benz, J., Bergner, A., Hofmann, A., Demange, P., Goettig, P., Liemann, S., Huber, R., & Voges, D. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0426 · Cited by 107 · see citing works
Annexin 11 is required for midbody formation and completion of the terminal phase of cytokinesis
Tomás, A., Futter, C. E., & Moss, S. E. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200311054 · Cited by 106 · see citing works
A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: characterization of a novel gut-specific N-myristoylated annexin.
Wice, B. M., & Gordon, J. I. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.116.2.405 · Cited by 105 · see citing works
Structure and Dynamics of a Helical Hairpin and Loop Region in Annexin 12: A Site-Directed Spin Labeling Study
Isas, J. M., Langen, R., Haigler, H. T., & Hubbell, W. L. (2002) · Biochemistry · doi:10.1021/bi011856z · Cited by 105 · see citing works
The annexin A2 system and vascular homeostasis
Flood, E. C., & Hajjar, K. A. (2011) · Vascular Pharmacology · doi:10.1016/j.vph.2011.03.003 · Cited by 103 · see citing works
Annexin VI Participates in the Formation of a Reversible, Membrane-Cytoskeleton Complex in Smooth Muscle Cells
Babiychuk, E. B., Palstra, R.-J. T. S., Schaller, J., Kämpfer, U., & Draeger, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.49.35191 · Cited by 101 · see citing works
A transmembrane form of annexin XII detected by site-directed spin labeling
Langen, R., Isas, J. M., Hubbell, W. L., & Haigler, H. T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.24.14060 · Cited by 99 · see citing works
Annexin A6—Linking Ca2+ signaling with cholesterol transport
Enrich, C., Rentero, C., de Muga, S. V., Reverter, M., Mulay, V., Wood, P., Köse, M., & Grewal, T. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.09.015 · Cited by 99 · see citing works
Expression and purification of recombinant annexin V for the detection of membrane alterations on apoptotic cells
Brumatti, G., Sheridan, C., & Martin, S. J. (2008) · Methods · doi:10.1016/j.ymeth.2007.11.010 · Cited by 94 · see citing works
Annexin V Interaction with Phosphatidylserine-Containing Vesicles at Low and Neutral pH
Köhler, G., Hering, U., Zschörnig, O., & Arnold, K. (1997) · Biochemistry · doi:10.1021/bi9703960 · Cited by 94 · see citing works
Molecular imaging of cell death
Saint‐Hubert, M. D., Prinsen, K., Mortelmans, L. A., Verbruggen, A., & Mottaghy, F. M. (2009) · Methods · doi:10.1016/j.ymeth.2009.03.022 · Cited by 93 · see citing works
Antiphospholipid Antibody-mediated Disruption of the Annexin-V Antithrombotic Shield: a Thrombogenic Mechanism for the Antiphospholipid Syndrome
Rand, J. H. (2000) · Journal of Autoimmunity · doi:10.1006/jaut.2000.0410 · Cited by 87 · see citing works
Participation of annexins in protein phosphorylation
Rothhut, B. (1997) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050066 · Cited by 83 · see citing works
Annexin A2 Is Involved in the Formation of Hepatitis C Virus Replication Complex on the Lipid Raft
Saxena, V., Lai, C.-K., Chao, T., Jeng, K.-S., & Lai, M. M. C. (2012) · Journal of Virology · doi:10.1128/jvi.06327-11 · Cited by 83 · see citing works
Phosphorylation Mutants Elucidate the Mechanism of Annexin IV-Mediated Membrane Aggregation,
Kaetzel, M. A., Mo, Y. D., Mealy, T. R., Campos, B., Bergsma‐Schutter, W., Brisson, A. R., Dedman, J. R., & Seaton, B. A. (2001) · Biochemistry · doi:10.1021/bi002507s · Cited by 83 · see citing works
Fluorescent Annexin A1 Reveals Dynamics of Ceramide Platforms in Living Cells
Babiychuk, E. B., Monastyrskaya, K., & Draeger, A. (2008) · Traffic · doi:10.1111/j.1600-0854.2008.00800.x · Cited by 82 · see citing works
Annexins V and XII Insert into Bilayers at Mildly Acidic pH and Form Ion Channels
Isas, J. M., Cartailler, J., Sokolov, Y., Patel, D. R., Langen, R., Luecke, H., Hall, J. E., & Haigler, H. T. (2000) · Biochemistry · doi:10.1021/bi9922401 · Cited by 82 · see citing works
Annexin V inhibits protein kinase C activity via a mechanism of phospholipid sequestration
Dubois, T., Mira, J. P., Féliers, D., Solito, E., Russo‐Marie, F., & Oudinet, J. (1998) · Biochemical Journal · doi:10.1042/bj3301277 · Cited by 79 · see citing works
Annexin A6 contributes to the invasiveness of breast carcinoma cells by influencing the organization and localization of functional focal adhesions
Sakwe, A. M., Koumangoye, R. B., Guillory, B., & Ochieng, J. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.12.008 · Cited by 79 · see citing works
Evolutionary perspective on annexin calcium-binding domains
Morgan, R. O., Martin‐Almedina, S., Iglesias, J. M., Gonzalez-Florez, M. I., & Fernández, M. P. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.09.010 · Cited by 79 · see citing works
Endonexin II, Present on Human Liver Plasma Membranes, Is a Specific Binding Protein of Small Hepatitis B Virus (HBV) Envelope Protein
Hertogs, K., Leenders, W. P. J., Depla, E., Bruin, W. C. C. D., Meheus, L., Raymackers, J., Moshage, H. J., & Yap, S. H. (1993) · Virology · doi:10.1006/viro.1993.1628 · Cited by 78 · see citing works
Annexin A6-regulator of the EGFR/Ras signalling pathway and cholesterol homeostasis
Grewal, T., Köse, M., Rentero, C., & Enrich, C. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.12.020 · Cited by 77 · see citing works
Annexin A6 inhibits Ras signalling in breast cancer cells
de Muga, S. V., Timpson, P., Cubells, L., Evans, R., Hayes, T. E., Rentero, C., Hegemann, A., Reverter, M., Leschner, J., Pol, A., et al. (2008) · Oncogene · doi:10.1038/onc.2008.386 · Cited by 76 · see citing works
Human Annexin A6 Interacts with Influenza A Virus Protein M2 and Negatively Modulates Infection
Ma, H., Kien, F., Manière, M., Zhang, Y., Lagarde, N., Tse, K. S., Poon, L. L. M., & Nal, B. (2011) · Journal of Virology · doi:10.1128/jvi.06003-11 · Cited by 73 · see citing works
Annexin A6 is a scaffold for PKCα to promote EGFR inactivation
Köse, M., Rentero, C., Kota, B. P., Hoque, M., Cairns, R. F., Wood, P., de Muga, S. V., Reverter, M., Álvarez-Guaita, A., Monastyrskaya, K., et al. (2012) · Oncogene · doi:10.1038/onc.2012.303 · Cited by 73 · see citing works
Evidence for a Role of the Adenosine 5′-Triphosphate-Binding Cassette Transporter A1 in the Externalization of Annexin I from Pituitary Folliculo-Stellate Cells
Chapman, L. P., Epton, M. J., Buckingham, J. C., Morris, J. F., & Christian, H. (2003) · Endocrinology · doi:10.1210/en.2002-220650 · Cited by 71 · see citing works
Annexin A6 is an organizer of membrane microdomains to regulate receptor localization and signalling
Cornely, R., Rentero, C., Enrich, C., Grewal, T., & Gaus, K. (2011) · IUBMB Life · doi:10.1002/iub.540 · Cited by 70 · see citing works
Multiple Roles of Annexin A2 in Post-Transcriptional Regulation of Gene Expressio
Vedeler, A., Hollås, H., Grindheim, A. K., & Raddum, A. M. (2012) · Current Protein and Peptide Science · doi:10.2174/138920312801619402 · Cited by 70 · see citing works
A New Consensus Sequence for Phosphatidylserine Recognition by Annexins
Montaville, P., Neumann, J., Russo‐Marie, F., Ochsenbein, F., & Sanson, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109595200 · Cited by 70 · see citing works
Reciprocal Regulation of Annexin A2 and EGFR with Her-2 in Her-2 Negative and Herceptin-Resistant Breast Cancer
Shetty, P. K., Thamake, S. I., Biswas, S., Johansson, S. L., & Vishwanatha, J. K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044299 · Cited by 68 · see citing works
Distinct Annexin Subfamilies in Plants and Protists Diverged Prior to Animal Annexins and from a Common Ancestor
Morgan, R. O., & Fernández, M. P. (1997) · Journal of Molecular Evolution · doi:10.1007/pl00006134 · Cited by 67 · see citing works
Detection of anti-annexin IV and V antibodies in patients with antiphospholipid syndrome and systemic lupus erythematosus.
Satoh, A., Suzuki, K., Takayama‐Muromachi, E., Kojima, K., Hidaka, T., Kawakami, M., Matsumoto, I., & Ohsuzu, F. (1999) · PubMed · Cited by 67 · see citing works
Crystal structure of bovine annexin VI in a calcium-bound state
Avila-Sakar, A., Creutz, C. E., & Kretsinger, R. H. (1998) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(98)00111-3 · Cited by 66 · see citing works
Novel Human and Mouse Annexin A10 Are Linked to the Genome Duplications during Early Chordate Evolution
Morgan, R. O., Jenkins, N. A., Gilbert, D. J., Copeland, N. G., Balsara, B., Testa, J. R., & Fernández, M. P. (1999) · Genomics · doi:10.1006/geno.1999.5895 · Cited by 65 · see citing works
Annexin II contains two types of Ca2+-binding sites
Jost, M., Weber, K., & Gerke, V. (1994) · Biochemical Journal · doi:10.1042/bj2980553 · Cited by 64 · see citing works
Unmasking the Annexin I Interaction from the Structure of Apo-S100A11
Rintala‐Dempsey, A. C., Walsh, M. P., & Shaw, G. S. (2003) · Structure · doi:10.1016/s0969-2126(03)00126-6 · Cited by 63 · see citing works
The effect of metal binding on the structure of annexin V and implications for membrane binding
Lewit‐Bentley, A., Moréra, S., Huber, R., & Bodo, G. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17392.x · Cited by 63 · see citing works
Annexin A2 at the interface between F-actin and membranes enriched in phosphatidylinositol 4,5,-bisphosphate
Hayes, M., Shao, D., Grieve, A., Levine, T. P., Bailly, M., & Moss, S. (2008) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamcr.2008.10.007 · Cited by 61 · see citing works
Annexin A5 inhibits engulfment through internalization of PS-expressing cell membrane patches
Kenis, H., van Genderen, H., Deckers, N. M., Lux, P., Hofstra, L., Narula, J., & Reutelingsperger, C. P. M. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.11.023 · Cited by 59 · see citing works
Interaction of annexins with membranes: The N-terminus as a governing parameter as revealed with a chimeric annexin
Hoekstra, D., Buist-Arkema, R., Klappe, K., & Reutelingsperger, C. P. M. (1993) · Biochemistry · doi:10.1021/bi00214a019 · Cited by 59 · see citing works
Acidic pH-induced folding of annexin VI is a prerequisite for its insertion into lipid bilayers and formation of ion channels by the protein molecules
Golczak, M., Kicińska, A., Bandorowicz‐Pikuła, J., Buchet, R., Szewczyk, A. M., & Pikuła, S. (2001) · The FASEB Journal · doi:10.1096/fj.00-0523fje · Cited by 59 · see citing works
Annexin V relocates to the platelet cytoskeleton upon activation and binds to a specific isoform of actin
Tzima, E., Trotter, P. J., Orchard, M. A., & Walker, J. H. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01525.x · Cited by 58 · see citing works
Structure of chicken annexin V at 2.25-.ANG. resolution
Bewley, M. C., Boustead, C. M., Walker, J. H., Waller, D. A., & Huber, R. (1993) · Biochemistry · doi:10.1021/bi00066a011 · Cited by 57 · see citing works
Ca2+‐independent interaction of annexin I with phospholipid monolayers
Rosengarth, A., Wintergalen, A., Galla, H., Hinz, H., & Gerke, V. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01318-0 · Cited by 55 · see citing works
Calcium and Membrane-Binding Properties of Monomeric and Multimeric Annexin II
Evans, T. C., & Nelsestuen, G. L. (1994) · Biochemistry · doi:10.1021/bi00249a009 · Cited by 54 · see citing works
Optimal Modification of Annexin V with Fluorescent Dyes
Schellenberger, E. A., Weissleder, R., & Josephson, L. (2004) · ChemBioChem · doi:10.1002/cbic.200300741 · Cited by 54 · see citing works
Structural and Functional Characterisation of the Voltage Sensor in the Ion Channel Human Annexin V
Liemann, S., Benz, J., Bürger, A., Voges, D., Hofmann, A., Huber, R., & Goettig, P. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0268 · Cited by 53 · see citing works
Annexin-A6 presents two modes of association with phospholipid membranes. A combined QCM-D, AFM and cryo-TEM study
Buzhynskyy, N., Golczak, M., Lai‐Kee‐Him, J., Lambert, O., Tessier, B., Gounou, C., Bérat, R., Simon, A., Granier, T., Chevalier, J.-M., et al. (2009) · Journal of Structural Biology · doi:10.1016/j.jsb.2009.03.007 · Cited by 52 · see citing works
Site-specific 68Ga-labeled Annexin A5 as a PET imaging agent for apoptosis
Bauwens, M., Saint‐Hubert, M. D., Devos, E., Deckers, N. M., Reutelingsperger, C. P. M., Mortelmans, L. A., Himmelreich, U., Mottaghy, F. M., & Verbruggen, A. (2010) · Nuclear Medicine and Biology · doi:10.1016/j.nucmedbio.2010.09.008 · Cited by 51 · see citing works
Mediation of annexin 1 secretion by a probenecid-sensitive ABC-transporter in rat inflamed mucosa
Wein, S., Fauroux, M., Laffitte, J., de Nadaı̈, P., Guaı̈ni, C., Pons, F., & Coméra, C. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2003.11.015 · Cited by 50 · see citing works
Membrane-Bound 3D Structures Reveal the Intrinsic Flexibility of Annexin VI
Avila-Sakar, A., Kretsinger, R. H., & Creutz, C. E. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4246 · Cited by 50 · see citing works
Phosphorylation of Annexin A1 by TRPM7 Kinase: A Switch Regulating the Induction of an α-Helix
Dorovkov, M. V., Kostyukova, A. S., & Ryazanov, A. G. (2011) · Biochemistry · doi:10.1021/bi101963h · Cited by 50 · see citing works
Annexin A6-induced Inhibition of Cytoplasmic Phospholipase A2 Is Linked to Caveolin-1 Export from the Golgi
Cubells, L., de Muga, S. V., Tebar, F., Bonventre, J. V., Balsinde, J., Pol, A., Grewal, T., & Enrich, C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706618200 · Cited by 49 · see citing works
Quantitative proteomic analysis of exosomes from HIV-1 infected lymphocytic cells
Li, M., Aliotta, J., Asara, J. M., Tucker, L., Quesenberry, P., Lally, M., & Ramratnam, B. (2012) · Proteomics · doi:10.1002/pmic.201100376 · Cited by 49 · see citing works
Annexin 2-mediated enhancement of cytomegalovirus infection opposes inhibition by annexin 1 or annexin 5
Derry, M. C., Sutherland, M. R., Restall, C. M., Waisman, D. M., & Pryzdial, E. L. G. (2006) · Journal of General Virology · doi:10.1099/vir.0.82294-0 · Cited by 48 · see citing works
Annexin A8 displays unique phospholipid and F‐actin binding properties
Goebeler, V., Ruhe, D., Gerke, V., & Rescher, U. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.03.076 · Cited by 47 · see citing works
Flippin' lipids
Clark, M. R. (2011) · Nature Immunology · doi:10.1038/ni.2024 · Cited by 45 · see citing works
Effects of profilin–annexin I association on some properties of both profilin and annexin I: modification of the inhibitory activity of profilin on actin polymerization and inhibition of the self-association of annexin I and its interactions with liposomes
Alvarez‐Martinez, M., Porte, F., Liautard, J., & Widada, J. S. (1997) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(97)00018-6 · Cited by 45 · see citing works
Characterization of the Interaction Between Annexin I and Profilin
Alvarez‐Martinez, M., Mani, J. C., Porte, F., Faivre‐Sarrailh, C., Liautard, J., & Widada, J. S. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0777w.x · Cited by 45 · see citing works
The music of lipids: How lipid composition orchestrates cellular behaviour
Schug, Z. T., Frezza, C., Galbraith, L. C. A., & Gottlieb, E. (2012) · Acta Oncologica · doi:10.3109/0284186x.2011.643823 · Cited by 44 · see citing works
Involvement of annexin V in the entry of influenza viruses and role of phospholipids in infection
Huang, R. T. C., Lichtenberg, B., & Rick, O. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00783-1 · Cited by 44 · see citing works
The Conserved Core Domains of Annexins A1, A2, A5, and B12 Can Be Divided into Two Groups with Different Ca2+-Dependent Membrane-Binding Properties
Patel, D. R., Isas, J. M., Ladokhin, A. S., Jao, C. C., Kim, Y., Kirsch, T., Langen, R., & Haigler, H. T. (2005) · Biochemistry · doi:10.1021/bi047642+ · Cited by 44 · see citing works
Cell attachment, collagen binding, and receptor analysis on bovine articular chondrocytes
Reid, D. L., Aydelotte, M. B., & Mollenhauer, J. A. (2000) · Journal of Orthopaedic Research® · doi:10.1002/jor.1100180307 · Cited by 44 · see citing works
Annexin A1 regulates hormone exocytosis through a mechanism involving actin reorganization
McArthur, S., Yazid, S., Christian, H., Sirha, R., Flower, R. J., Buckingham, J. C., & Solito, E. (2009) · The FASEB Journal · doi:10.1096/fj.09-131391 · Cited by 42 · see citing works
Structure–function relationship in annexin A13, the founder member of the vertebrate family of annexins
Turnay, J., Lecona, E., Fernández‐Lizarbe, S., Guzmán‐Aránguez, A., Fernández, M. P., Olmo, N., & Lizarbe, M. A. (2005) · Biochemical Journal · doi:10.1042/bj20041918 · Cited by 41 · see citing works
Self-citation
Collagen/Annexin V Interactions Regulate Chondrocyte Mineralization
Kim, H. J., & Kirsch, T. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708456200 · Cited by 40 · see citing works
Structure of an Asymmetric Ternary Protein Complex Provides Insight for Membrane Interaction
Dempsey, B. R., Rezvanpour, A., Lee, T.-W., Barber, K. R., Junop, M. S., & Shaw, G. S. (2012) · Structure · doi:10.1016/j.str.2012.08.004 · Cited by 39 · see citing works
Structural Determinant of the Vesicle Aggregation Activity of Annexin I
Bitto, E., & Cho, W. (1999) · Biochemistry · doi:10.1021/bi990457p · Cited by 39 · see citing works
Anx2 Interacts with HIV-1 Gag at Phosphatidylinositol (4,5) Bisphosphate-Containing Lipid Rafts and Increases Viral Production in 293T Cells
Harrist, A. V., Ryzhova, E. V., Harvey, T. S., & González‐Scarano, F. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005020 · Cited by 38 · see citing works
Inhibition of secreted phospholipases A2 by annexin V. Competition for anionic phospholipid interfaces allows an assessment of the relative interfacial affinities of secreted phospholipases A2
Buckland, A. G., & Wilton, D. C. (1998) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/s0005-2760(98)00026-5 · Cited by 37 · see citing works
Essential Role of B-helix Calcium Binding Sites in Annexin V-Membrane Binding
Jin, M., Smith, C., Hsieh, H.-Y., Gibson, D. F., & Tait, J. F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405846200 · Cited by 37 · see citing works
Structural and functional characterization of recombinant mouse annexin A11: influence of calcium binding
Lecona, E., Turnay, J., Olmo, N., Guzmán‐Aránguez, A., Morgan, R. O., Fernández, M. P., & Lizarbe, M. A. (2003) · Biochemical Journal · doi:10.1042/bj20021721 · Cited by 35 · see citing works
Self-citation
Protection of the Membrane Permeability Barrier by Annexins
Creutz, C. E., Hira, J. K., Gee, V. E., & Eaton, J. M. (2012) · Biochemistry · doi:10.1021/bi3013559 · Cited by 34 · see citing works
The N-terminal Domain of Annexin 2 Serves as a Secondary Binding Site during Membrane Bridging
Zibouche, M., Vincent, M., Illien, F., Gallay, J., & Ayala‐Sanmartín, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801000200 · Cited by 32 · see citing works
Cell surface annexins regulate ADAM-mediated ectodomain shedding of proamphiregulin
Nakayama, H., Fukuda, S., Inoue, H., Nishida‐Fukuda, H., Shirakata, Y., Hashimoto, K., & Higashiyama, S. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-08-0683 · Cited by 32 · see citing works
Conformational Flexibility of Domain III of Annexin V Studied by Fluorescence of Tryptophan 187 and Circular Dichroism: The Effect of PH
Santos, J. S. O., Vincent, M., Takahashi, M., Lewit‐Bentley, A., & Gallay, J. (1998) · Biochemistry · doi:10.1021/bi980773o · Cited by 32 · see citing works
Structural and Dynamic Changes in Human Annexin VI Induced by a Phosphorylation-Mimicking Mutation, T356D,
Freye-Minks, C., Kretsinger, R. H., & Creutz, C. E. (2002) · Biochemistry · doi:10.1021/bi026742h · Cited by 31 · see citing works
Presence and Comparison of Ca2+Transport Activity of Annexins I, II, V, and VI in Large Unilamellar Vesicles
Matsuda, R., Kaneko, N., & Horikawa, Y. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7177 · Cited by 31 · see citing works
Change in the N-terminal domain conformation of annexin I that correlates with liposome aggregation is impaired by Ser-27 to Glu mutation that mimics phosphorylation
Porte, F., Barbara, P. D. S., Phalipou, S., Liautard, J., & Widada, J. S. (1996) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(95)00220-0 · Cited by 29 · see citing works
Calcium-Dependent Conformational Rearrangements and Protein Stability in Chicken Annexin A5
Turnay, J., Olmo, N., Gasset, M., Iloro, I., Arrondo, J. L. R., & Lizarbe, M. A. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)73988-x · Cited by 29 · see citing works
Self-citation
Formation of irreversibly bound annexin A1 protein domains on POPC/POPS solid supported membranes
Faiß, S., Kastl, K., Janshoff, A., & Steinem, C. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.01.003 · Cited by 29 · see citing works
Voltage dependent binding of annexin V, annexin VI and annexin VII-core to acidic phospholipid membranes
Hofmann, A., Benz, J., Liemann, S., & Huber, R. (1997) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(97)00150-8 · Cited by 28 · see citing works
Annexin A9 is a periplakin interacting partner in membrane‐targeted cytoskeletal linker protein complexes
Boczonadi, V., & Määttå, A. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.07.057 · Cited by 27 · see citing works
Insight into the location and dynamics of the annexin A2 N-terminal domain during Ca2+-induced membrane bridging
Ayala‐Sanmartín, J., Zibouche, M., Illien, F., Vincent, M., & Gallay, J. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.11.004 · Cited by 27 · see citing works
Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca2+ and lipid binding proteins
Goebeler, V., Ruhe, D., Gerke, V., & Rescher, U. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00634-3 · Cited by 26 · see citing works
Dissecting the Cellular Functions of Annexin XI Using Recombinant Human Annexin XI-specific Autoantibodies Cloned by Phage Display
Farnaes, L., & Ditzel, H. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210852200 · Cited by 26 · see citing works
Modulation by Ca2+ and by Membrane Binding of the Dynamics of Domain III of Annexin 2 (p36) and the Annexin 2−p11 Complex (p90): Implications for Their Biochemical Properties
Ayala‐Sanmartín, J., Vincent, M., Santos, J. S. O., & Gallay, J. (2000) · Biochemistry · doi:10.1021/bi000501x · Cited by 26 · see citing works
Antibody-mediated interference with annexins in the antiphospholipid syndrome
Rand, J. H., & Wu, X.-X. (2004) · Thrombosis Research · doi:10.1016/j.thromres.2004.07.021 · Cited by 25 · see citing works
Acid induced equilibrium unfolding of annexin V wild type shows two intermediate states
BEERMANN, B. B., Hinz, H., Hofmann, A., & Huber, R. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00105-7 · Cited by 25 · see citing works
Role of the N‐terminus in the structure and stability of chicken annexin V
Arboledas, D., Olmo, N., Lizarbe, M. A., & Turnay, J. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01207-6 · Cited by 25 · see citing works
Self-citation
Annexin V-crystal structure and its implications on function.
Huber, R., Berendes, R., Bürger, A., Luecke, H., & Karshikov, A. (1992) · PubMed · Cited by 25 · see citing works
Do annexins participate in lipid messenger mediated intracellular signaling? A question revisited
Bandorowicz‐Pikuła, J., Woś, M., & Pikuła, S. (2012) · Molecular Membrane Biology · doi:10.3109/09687688.2012.693210 · Cited by 24 · see citing works
Calcium-Dependent Binding of Annexin 12 to Phospholipid Bilayers: Stoichiometry and Implications
Patel, D. R., Jao, C. C., Mailliard, W. S., Isas, J. M., Langen, R., & Haigler, H. T. (2001) · Biochemistry · doi:10.1021/bi010345+ · Cited by 24 · see citing works
Collagen binding activity of recombinant and N‐terminally modified annexin V (anchorin CII)
Turnay, J., Pfannmüller, E., Lizarbe, M. A., Bertling, W. M., & von der Mark, K. (1995) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240580210 · Cited by 23 · see citing works
Self-citation
Lipid organization regulates annexin A2 Ca2+-sensitivity for membrane bridging and its modulator effects on membrane fluidity
Illien, F., Piao, H.-R., Coué, M., di Marco, C., & Ayala‐Sanmartín, J. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.07.012 · Cited by 23 · see citing works
Structure of Human Annexin A6 at the Air-Water Interface and in a Membrane-Bound State
Golczak, M., Kirilenko, A., Bandorowicz‐Pikuła, J., Desbat, B., & Pikuła, S. (2004) · Biophysical Journal · doi:10.1529/biophysj.103.038240 · Cited by 23 · see citing works
A Helical Hairpin Region of Soluble Annexin B12 Refolds and Forms a Continuous Transmembrane Helix at Mildly Acidic pH
Kim, Y., Isas, J. M., Haigler, H. T., & Langen, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505017200 · Cited by 22 · see citing works
Membrane-Induced Folding and Structure of Membrane-Bound Annexin A1 N-Terminal Peptides: Implications for Annexin-Induced Membrane Aggregation
Hu, N., Bradshaw, J., Lauter, H., Buckingham, J. C., Solito, E., & Hofmann, A. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.119685 · Cited by 21 · see citing works
Binding to phosphatidyl serine membranes causes a conformational change in the concave face of annexin I
de la Fuente, M., & Ossa, C. G. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78677-6 · Cited by 20 · see citing works
Global Structural Changes in Annexin 12
Isas, J. M., Patel, D. R., Jao, C. C., Jayasinghe, S. A., Cartailler, J., Haigler, H. T., & Langen, R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301228200 · Cited by 20 · see citing works
Molecular dynamics simulation studies on Ca2+-induced conformational changes of annexin I
Shesham, R. D., Bartolotti, L. J., & Li, Y. (2008) · Protein Engineering Design and Selection · doi:10.1093/protein/gzm094 · Cited by 19 · see citing works
A Novel Calcium-Independent Peripheral Membrane-Bound Form of Annexin B12
Hegde, B. G., Isas, J. M., Zampighi, G. A., Haigler, H. T., & Langen, R. (2005) · Biochemistry · doi:10.1021/bi052143+ · Cited by 18 · see citing works
Different molecular arrangements of the tetrameric annexin 2 modulate the size and dynamics of membrane aggregation
Illien, F., Finet, S., Lambert, O., & Ayala‐Sanmartín, J. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.05.001 · Cited by 17 · see citing works
Annexin A4 binding to anionic phospholipid vesicles modulated by pH and calcium
Zschörnig, O., Opitz, F., & Müller, M. (2007) · European Biophysics Journal · doi:10.1007/s00249-007-0147-1 · Cited by 17 · see citing works
Partial truncation of the NH2-terminus affects physical characteristics and membrane binding, aggregation, and fusion properties of annexin A7
Naidu, D. G., Raha, A., Chen, X.-L., Spitzer, A. R., & Chander, A. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2005.03.007 · Cited by 15 · see citing works
Secretion of Annexin V from Cultured Cells Requires a Signal Peptide
Wang, X., Campos, B., Kaetzel, M. A., & Dedman, J. R. (2001) · Placenta · doi:10.1053/plac.2001.0724 · Cited by 14 · see citing works
Role of Intracellular Proteins in the Regulation of Calcium Action and Transmitter Release During Exocytosis
Pollard, H. B., Pazoles, C. J., Creutz, C. E., & Zinder, O. (2015) · Monographs in clinical neuroscience/Frontiers of neurology and neuroscience/Monographs in neural sciences · doi:10.1159/000388818 · Cited by 12 · see citing works
Calcium- and Membrane-Induced Changes in the Structure and Dynamics of Three Helical Hairpins in Annexin B12
Isas, J. M., Kim, Y., Jao, C. C., Hegde, P. B., Haigler, H. T., & Langen, R. (2005) · Biochemistry · doi:10.1021/bi051751m · Cited by 11 · see citing works
Mycobacteria-containing phagosomes associate less annexins I, VI, VII and XI, but not II, concomitantly with a diminished phagolysosomal fusion
Pittis, M. G., Muzzolini, L., Giulianini, P. G., & Garcia, R. C. (2003) · European Journal of Cell Biology · doi:10.1078/0171-9335-00293 · Cited by 10 · see citing works
New force field for calcium binding sites in annexin–membrane complexes
Merzel, F., Hodošček, M., Janežič, D., & Sanson, A. (2006) · Journal of Computational Chemistry · doi:10.1002/jcc.20340 · Cited by 10 · see citing works
Key role of the N‐terminus of chicken annexin A5 in vesicle aggregation
Turnay, J., Guzmán‐Aránguez, A., Lecona, E., Barrasa, J. I., Olmo, N., & Lizarbe, M. A. (2009) · Protein Science · doi:10.1002/pro.119 · Cited by 7 · see citing works
Self-citation
Untitled work
(1998) · doi:10.1002/(sici)1097-0320(19980101)31:1

Flagged first, then by citations

2 of the 173 references couldn’t be matched to a known paper.

Research works printed but not linked: 1

[22]Rosengarth A. Gerke V. Luecke H. X-ray structure of full-length annexin 1 and implications for membrane aggregation J. Mol. Biol 2001 306 489 498 11178908

Sorted by citations

Calcium transport across plant membranes: mechanisms and functions
Demidchik, V. V., Shabala, S. N., Isayenkov, S. V., Cuin, T. A., & Pottosin, I. I. (2018) · New Phytologist · doi:10.1111/nph.15266 · Cited by 458 · see citing works
MSC secretes at least 3 EV types each with a unique permutation of membrane lipid, protein and RNA
Lai, R. C., Tan, S. S., Yeo, R. W. Y., Choo, A. B. H., Reiner, A. T., Su, Y. P., Shen, Y., Fu, Z., Lezhava, A., Sze, S. K., et al. (2016) · Journal of Extracellular Vesicles · doi:10.3402/jev.v5.29828 · Cited by 259 · see citing works
Semen proteomics and male infertility
Jodar, M., Soler‐Ventura, A., & Oliva, R. (2016) · Journal of Proteomics · doi:10.1016/j.jprot.2016.08.018 · Cited by 194 · see citing works
Unconventional secretion of annexins and galectins
Popa, S. J., Stewart, S. E., & Moreau, K. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.02.022 · Cited by 167 · see citing works
An actin-dependent annexin complex mediates plasma membrane repair in muscle
Demonbreun, A. R., Quattrocelli, M., Barefield, D. Y., Allen, M. V., Swanson, K. E., & McNally, E. M. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201512022 · Cited by 180 · see citing works
ROS-Activated Ion Channels in Plants: Biophysical Characteristics, Physiological Functions and Molecular Nature
Demidchik, V. V. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19041263 · Cited by 171 · see citing works
Profiling the human hippocampal proteome at all pathologic stages of Alzheimer's disease
Hondius, D., van Nierop, P., Li, K. W., Hoozemans, J. J. M., van der Schors, R. C., van Haastert, E. S., van der Vies, S. M., Rozemüller, A. J. M., & Smit, A. B. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2015.11.002 · Cited by 165 · see citing works
Mechanisms of cytosolic calcium elevation in plants: the role of ion channels, calcium extrusion systems and NADPH oxidase-mediated ‘ROS-Ca2+ Hub’
Demidchik, V. V., & Shabala, S. N. (2017) · Functional Plant Biology · doi:10.1071/fp16420 · Cited by 158 · see citing works
Multi-Omics Analysis of Microglial Extracellular Vesicles From Human Alzheimer’s Disease Brain Tissue Reveals Disease-Associated Signatures
Cohn, W., Melnik, M., Huang, C., Teter, B., Chandra, S., Zhu, C., McIntire, L. B., John, V., Gylys, K. H., & Bilousova, T. V. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.766082 · Cited by 120 · see citing works
Annexin-V stabilizes membrane defects by inducing lipid phase transition
Lin, Y., Chipot, C. J., & Simon Scheuring, A. (2020) · Nature Communications · doi:10.1038/s41467-019-14045-w · Cited by 117 · see citing works
Phospholipase D and phosphatidic acid in the biogenesis and cargo loading of extracellular vesicles
Egea-Jiménez, A. L., & Zimmermann, P. (2018) · Journal of Lipid Research · doi:10.1194/jlr.r083964 · Cited by 115 · see citing works
ECM deposition is driven by caveolin-1–dependent regulation of exosomal biogenesis and cargo sorting
Albacete-Albacete, L., Navarro‐Lérida, I., López, J. A., Martín-Padura, I., Astudillo, A. M., Ferrarini, A., van der Heyden, M., Balsinde, J., Orend, G., Vázquez, J., et al. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202006178 · Cited by 115 · see citing works
The Phagocytic Code Regulating Phagocytosis of Mammalian Cells
Cockram, T. O. J., Dundee, J. M., Popescu, A. S., & Brown, G. C. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.629979 · Cited by 111 · see citing works
Annexin A5 as a potential marker in tumors
Peng, B., Guo, C., Guan, H., Liu, S., & Sun, M. (2013) · Clinica Chimica Acta · doi:10.1016/j.cca.2013.09.048 · Cited by 109 · see citing works
High-speed atomic force microscopy shows that annexin V stabilizes membranes on the second timescale
Miyagi, A., Chipot, C. J., Rangl, M., & Simon Scheuring, A. (2016) · Nature Nanotechnology · doi:10.1038/nnano.2016.89 · Cited by 107 · see citing works
Cell-surface phosphatidylserine regulates osteoclast precursor fusion
Verma, S. K., Leikina, E., Melikov, K., Gebert, C. M., Kram, V., Young, M. F., Uygur, B., & Chernomordik, L. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.809681 · Cited by 104 · see citing works
Roles and Regulation of Extracellular Vesicles in Cardiovascular Mineral Metabolism
Blaser, M. C., & Aïkawa, E. (2018) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2018.00187 · Cited by 101 · see citing works
Annexins induce curvature on free-edge membranes displaying distinct morphologies
Boye, T. L., Jeppesen, J. C., Maeda, K., Pezeshkian, W., Solovyeva, V., Nylandsted, J., & Simonsen, A. C. (2018) · Scientific Reports · doi:10.1038/s41598-018-28481-z · Cited by 99 · see citing works
Exosomal Proteins and Lipids as Potential Biomarkers for Lung Cancer Diagnosis, Prognosis, and Treatment
Hsu, M.-T., Wang, Y.-K., & Tseng, Y. J. (2022) · Cancers · doi:10.3390/cancers14030732 · Cited by 94 · see citing works
Anion recognition by cyclic peptides
Elmes, R. B. P., & Jolliffe, K. A. (2015) · Chemical Communications · doi:10.1039/c4cc10095f · Cited by 84 · see citing works
Microscopic Imaging Techniques for Molecular Assemblies: Electron, Atomic Force, and Confocal Microscopies
Kubota, R., Tanaka, W., & Hamachi, I. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01334 · Cited by 82 · see citing works
Annexin A2 facilitates endocytic trafficking of antisense oligonucleotides
Wang, S., Sun, H., Tanowitz, M., Liang, X., & Crooke, S. T. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw595 · Cited by 72 · see citing works
Discovery of a non-cationic cell penetrating peptide derived from membrane-interacting human proteins and its potential as a protein delivery carrier
Kim, H. Y., Yum, S., Jang, G., & Ahn, D. (2015) · Scientific Reports · doi:10.1038/srep11719 · Cited by 70 · see citing works
From Proteomic Analysis to Potential Therapeutic Targets: Functional Profile of Two Lung Cancer Cell Lines, A549 and SW900, Widely Studied in Pre-Clinical Research
Korrodi‐Gregório, L., Soto‐Cerrato, V., Vitorino, R. M. P., Fardilha, M., & Pérez‐Tomás, R. (2016) · PLoS ONE · doi:10.1371/journal.pone.0165973 · Cited by 69 · see citing works
OsANN3, a calcium-dependent lipid binding annexin is a positive regulator of ABA-dependent stress tolerance in rice
Li, X., Zhang, Q., Yang, X., Han, J., & Zhu, Z. (2019) · Plant Science · doi:10.1016/j.plantsci.2019.04.019 · Cited by 69 · see citing works
Roles of Farnesyl-Diphosphate Farnesyltransferase 1 in Tumour and Tumour Microenvironments
Hà, N. T. T., & Lee, C. H. (2020) · Cells · doi:10.3390/cells9112352 · Cited by 71 · see citing works
Ca2+-dependent repair of pneumolysin pores: A new paradigm for host cellular defense against bacterial pore-forming toxins
Wolfmeier, H., Schoenauer, R., Atanassoff, A. P., Neill, D. R., Kadioglu, A., Draeger, A., & Babiychuk, E. B. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.09.005 · Cited by 65 · see citing works
Design and Synthesis of Multi-Functional Superparamagnetic Core-Gold Shell Nanoparticles Coated with Chitosan and Folate for Targeted Antitumor Therapy
Al-Musawi, S., Albukhaty, S., Al-Karagoly, H., & AlMalki, F. A. (2020) · Nanomaterials · doi:10.3390/nano11010032 · Cited by 64 · see citing works
Annexins as Overlooked Regulators of Membrane Trafficking in Plant Cells
Konopka‐Postupolska, D., & Clark, G. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18040863 · Cited by 62 · see citing works
A fluorogenic BODIPY molecular rotor as an apoptosis marker
Ashokkumar, P., Ashoka, A. H., Collot, M., Das, A., & Klymchenko, A. S. (2019) · Chemical Communications · doi:10.1039/c9cc03242h · Cited by 62 · see citing works
Lactobacillus species inhibitory effect on colorectal cancer progression through modulating the Wnt/β-catenin signaling pathway
Ghanavati, R., Akbari, A., Mohammadi, F., Asadollahi, P., Javadi, A., Talebi, M., & Rohani, M. (2020) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-020-03740-8 · Cited by 64 · see citing works
Regulation of the Equilibrium between Closed and Open Conformations of Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding
Ecsédi, P., Kiss, B., Gógl, G., Radnai, L., Buday, L., Koprivanacz, K., Liliom, K., Leveles, I., Vértessy, B. G., Jeszenői, N., et al. (2017) · Structure · doi:10.1016/j.str.2017.06.001 · Cited by 60 · see citing works
The Role of Glycosyltransferases in Colorectal Cancer
Fernandez-Ponce, C. M., Geribaldi‐Doldán, N., Sánchez-Gomar, I., Quiroz, R. N., Ibarra, L. A., Escorcia, L. G., Fernández-Cisnal, R., Aroca, G., Garcia-Cozar, F. J., & Quiroz, E. N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115822 · Cited by 59 · see citing works
Annexins A1 and A2 are recruited to larger lysosomal injuries independently of ESCRTs to promote repair
Yim, W. W., Yamamoto, H., & Mizushima, N. (2022) · FEBS Letters · doi:10.1002/1873-3468.14329 · Cited by 59 · see citing works
Annexin V‐Modified Platelet‐Biomimetic Nanomedicine for Targeted Therapy of Acute Ischemic Stroke
Quan, X., Han, Y., Lu, P., Ding, Y., Wang, Q., Li, Y., Wei, J., Huang, Q., Wang, R., & Zhao, Y. (2022) · Advanced Healthcare Materials · doi:10.1002/adhm.202200416 · Cited by 57 · see citing works
Green synthesis of bacterial mediated anti-proliferative gold nanoparticles: inducing mitotic arrest (G2/M phase) and apoptosis (intrinsic pathway)
Kumar, C. G., Poornachandra, Y., & Chandrasekhar, C. (2015) · Nanoscale · doi:10.1039/c5nr04577k · Cited by 56 · see citing works
Annexin5 Plays a Vital Role in Arabidopsis Pollen Development via Ca2+-Dependent Membrane Trafficking
Zhu, J., Wu, X., Yuan, S., Qian, D., Nan, Q., An, L., & Xiang, Y. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102407 · Cited by 56 · see citing works
Design and synthesize of folate decorated Fe3O4@Au-DEX-CP nano formulation for targeted drug delivery in colorectal cancer therapy: In vitro and in vivo studies
Alnasraui, A. H. F., Joe, I. H., & Al-Musawi, S. (2023) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2023.104798 · Cited by 55 · see citing works
Uncompensated Polychromatic Analysis of Mitochondrial Membrane Potential Using JC‐1 and Multilaser Excitation
Biasi, S. D., Gibellini, L., & Cossarizza, A. (2015) · Current Protocols in Cytometry · doi:10.1002/0471142956.cy0732s72 · Cited by 54 · see citing works
Seminal Plasma Proteome as an Indicator of Sperm Dysfunction and Low Sperm Motility in Chickens
Li, Y., Sun, Y., Ni, A., Shi, L., Wang, P., Isa, A. M., Ge, P., Jiang, L., Fan, J., Ma, H., et al. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra120.002017 · Cited by 46 · see citing works
Annexin A5 as a targeting agent for cancer treatment
Woodward, A., Faria, G. N. F., & Harrison, R. G. (2022) · Cancer Letters · doi:10.1016/j.canlet.2022.215857 · Cited by 43 · see citing works
Proteomic analysis of fibroblastema formation in regenerating hind limbs of Xenopus laevis froglets and comparison to axolotl
Rao, N., Song, F., Jhamb, D., Wang, M., Milner, D. J., Price, N. M., Belecky‐Adams, T. L., Palakal, M. J., Cameron, J. A., Li, B., et al. (2014) · BMC Developmental Biology · doi:10.1186/1471-213x-14-32 · Cited by 43 · see citing works
Advances in cancer treatment: a new therapeutic target, Annexin A2
Li, Z., Yu, L., Hu, B., Chen, L., Jv, M., Wang, L., Zhou, C., Wei, M., & Zhao, L. (2021) · Journal of Cancer · doi:10.7150/jca.55173 · Cited by 43 · see citing works
Muscle Cells Fix Breaches by Orchestrating a Membrane Repair Ballet
Barthélémy, F., Defour, A., Lévy, N., Krahn, M., & Bartoli, M. (2018) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-170251 · Cited by 40 · see citing works
Annexin A4 trimers are recruited by high membrane curvatures in giant plasma membrane vesicles
Florentsen, C. D., Sonne, A., Moreno-Pescador, G., Pezeshkian, W., Zanjani, A. A. H., Khandelia, H., Nylandsted, J., & Bendix, P. M. (2020) · Soft Matter · doi:10.1039/d0sm00241k · Cited by 40 · see citing works
Structural insights into the T 6 SS effector protein Tse 3 and the Tse 3– Tsi 3 complex from P seudomonas aeruginosa reveal a calcium‐dependent membrane‐binding mechanism
Lu, D., Shang, G., Zhang, H., Yu, Q., Cong, X., Yuan, J., He, F., Zhu, C., Zhao, Y., Yin, K., et al. (2014) · Molecular Microbiology · doi:10.1111/mmi.12616 · Cited by 39 · see citing works
Curvature- and Phase-Induced Protein Sorting Quantified in Transfected Cell-Derived Giant Vesicles
Moreno-Pescador, G., Florentsen, C. D., Østbye, H., Sønder, S. L., Boye, T. L., Veje, E. L., Sonne, A., Semsey, S., Nylandsted, J., Daniels, R., et al. (2019) · ACS Nano · doi:10.1021/acsnano.9b01052 · Cited by 36 · see citing works
Annexin A3 and cancer (Review)
Liu, C., Li, N., Liu, G., & Feng, X. (2021) · Oncology Letters · doi:10.3892/ol.2021.13095 · Cited by 36 · see citing works
N-dihydrogalactochitosan as immune and direct antitumor agent amplifying the effects of photodynamic therapy and photodynamic therapy-generated vaccines
Korbelik, M., Banáth, J. P., Zhang, W., Gallagher, P., Hode, T., Lam, S. S. K., & Chen, W. R. (2019) · International Immunopharmacology · doi:10.1016/j.intimp.2019.105764 · Cited by 35 · see citing works
Insights into Membrane Curvature Sensing and Membrane Remodeling by Intrinsically Disordered Proteins and Protein Regions
Has, C., Sivadas, P., & Das, S. L. (2022) · The Journal of Membrane Biology · doi:10.1007/s00232-022-00237-x · Cited by 35 · see citing works
Membrane lipids define small extracellular vesicle subtypes secreted by mesenchymal stromal cells
Lai, R. C., & Lim, S. K. (2018) · Journal of Lipid Research · doi:10.1194/jlr.r087411 · Cited by 35 · see citing works
Diagnostic and Therapeutic Approaches for Glioblastoma and Neuroblastoma Cancers Using Chlorotoxin Nanoparticles
Boltman, T., Meyer, M., & Ekpo, O. E. (2023) · Cancers · doi:10.3390/cancers15133388 · Cited by 34 · see citing works
Real-time glioblastoma tumor microenvironment assessment by SpiderMass for improved patient management
Zirem, Y., Ledoux, L., Roussel, L., Maurage, C., Tirilly, P., Rhun, É. L., Meresse, B., Yagnik, G. B., Lim, M. J., Rothschild, K. J., et al. (2024) · Cell Reports Medicine · doi:10.1016/j.xcrm.2024.101482 · Cited by 34 · see citing works
Lipids in Exosome Biology
Egea-Jiménez, A. L., & Zimmermann, P. (2019) · Handbook of experimental pharmacology · doi:10.1007/164_2019_220 · Cited by 33 · see citing works
Salinity‐induced transcriptome profiles in marine and freshwater threespine stickleback after an abrupt 6‐hour exposure
Taugbøl, A., Solbakken, M. H., Jakobsen, K. S., & Vøllestad, L. A. (2022) · Ecology and Evolution · doi:10.1002/ece3.9395 · Cited by 33 · see citing works
Efficient and highly reproducible production of red blood cell-derived extracellular vesicle mimetics for the loading and delivery of RNA molecules
Biagiotti, S., Canonico, B., Tiboni, M., Abbas, F., Perla, E., Montanari, M., Battistelli, M., Papa, S., Casettari, L., Rossi, L., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-65623-y · Cited by 32 · see citing works
The Cytoskeletal Adaptor Obscurin-Like 1 Interacts with the Human Papillomavirus 16 (HPV16) Capsid Protein L2 and Is Required for HPV16 Endocytosis
Wüstenhagen, E., Hampe, L., Boukhallouk, F., Schneider, M. A., Spoden, G. A., Negwer, I., Koynov, K., Kast, W. M., & Florin, L. (2016) · Journal of Virology · doi:10.1128/jvi.01222-16 · Cited by 31 · see citing works
Novel Immune Stimulant Amplifies Direct Tumoricidal Effect of Cancer Ablation Therapies and Their Systemic Antitumor Immune Efficacy
Korbelik, M., Hode, T., Lam, S. S. K., & Chen, W. R. (2021) · Cells · doi:10.3390/cells10030492 · Cited by 31 · see citing works
Transbilayer phospholipid movement facilitates the translocation of annexin across membranes
Stewart, S. E., Ashkenazi, A., Williamson, A., Rubinsztein, D. C., & Moreau, K. (2018) · Journal of Cell Science · doi:10.1242/jcs.217034 · Cited by 30 · see citing works
Therapeutic Potential of Annexins in Sepsis and COVID-19
Mui, L., Martin, C. M., Tschirhart, B. J., & Feng, Q. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.735472 · Cited by 30 · see citing works
Directional Secretomes Reflect Polarity-Specific Functions in an In Vitro Model of Human Bronchial Epithelium
Pillai, D. K., Sankoorikal, B.-J., Johnson, E., Seneviratne, A. N., Zurko, J., Brown, K. J., Hathout, Y., & Rose, M. C. (2013) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2013-0188oc · Cited by 30 · see citing works
Characterization of Annexin V Fusion with the Superfolder GFP in Liposomes Binding and Apoptosis Detection
Abbady, A. Q., Twair, A., Ali, B., & Murad, H. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00317 · Cited by 30 · see citing works
Helicobacter pylori binds human Annexins via Lipopolysaccharide to interfere with Toll-like Receptor 4 signaling
Schmidinger, B., Petri, K., Lettl, C., Li, H., Namineni, S., Ishikawa-Ankerhold, H. C., Soto, L. F. J., & Haas, R. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010326 · Cited by 28 · see citing works
Antibodies to variable surface antigens induce antigenic variation in the intestinal parasite Giardia lamblia
Tenaglia, A. H., Luján, L. A., Ríos, D. N., Molina, C. R., Midlej, V. D. V. P., Iribarren, P. A., Berazategui, M. A., Torri, A., Saura, A., Peralta, D. O., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38317-8 · Cited by 28 · see citing works
Bioluminescence Resonance Energy Transfer (BRET)‐coupled Annexin V‐functionalized Quantum Dots for Near‐Infrared Optical Detection of Apoptotic Cells
Tsuboi, S., & Jin, T. (2017) · ChemBioChem · doi:10.1002/cbic.201700486 · Cited by 28 · see citing works
Advanced Microscopy Reveals Complex Developmental and Subcellular Localization Patterns of ANNEXIN 1 in Arabidopsis
Tichá, M., Richter, H., Ovečka, M., Maghelli, N., Hrbáčková, M., Dvořák, P., Šamaj, J., & Šamajová, O. (2020) · Frontiers in Plant Science · doi:10.3389/fpls.2020.01153 · Cited by 26 · see citing works
Annexin A1 , A2 , A5, and A6 involvement in human pathologies
Ferreira, L. P. D. S., da Silva, R. A., Gil, C. D., & Geisow, M. J. (2023) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26512 · Cited by 26 · see citing works
Annexins: Ca2+ Effectors Determining Membrane Trafficking in the Late Endocytic Compartment
Enrich, C., Rentero, C., Meneses‐Salas, E., Tebar, F., & Grewal, T. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-55858-5_14 · Cited by 26 · see citing works
Structure Determination of the Transactivation Domain of p53 in Complex with S100A4 Using Annexin A2 as a Crystallization Chaperone
Ecsédi, P., Gógl, G., Hóf, H., Kiss, B., Harmat, V., & Nyitray, L. (2020) · Structure · doi:10.1016/j.str.2020.05.001 · Cited by 26 · see citing works
The Relevance, Predictability, and Utility of Annexin A5 for Human Physiopathology
Jing, J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052865 · Cited by 24 · see citing works
The role of annexin A1 in Candida albicans and Candida auris infections in murine neutrophils
Sanches, J. M., Rossato, L. L., Lice, I., Fernandes, A. M. A. P., Duarte, G. H. B., Silva, A., Porcari, A. M., Carvalho, P. D. O., & Gil, C. D. (2020) · Microbial Pathogenesis · doi:10.1016/j.micpath.2020.104689 · Cited by 23 · see citing works
Reduced Annexin A3 in schizophrenia
Joaquim, H. P. G., Costa, A. C., Serpa, M. H., Talib, L. L., & Gattaz, W. F. (2019) · European Archives of Psychiatry and Clinical Neuroscience · doi:10.1007/s00406-019-01048-3 · Cited by 23 · see citing works
Annexins A1 and A2 Accumulate and Are Immobilized at Cross-Linked Membrane–Membrane Interfaces
Klenow, M. B., Iversen, C., Lund, F. W., Mularski, A., Heitmann, A. S. B., Dias, C., Nylandsted, J., & Simonsen, A. C. (2021) · Biochemistry · doi:10.1021/acs.biochem.1c00126 · Cited by 23 · see citing works
ETV4 mediates the Wnt/β-catenin pathway through transcriptional activation of ANXA2 to promote hepatitis B virus-associated liver hepatocellular carcinoma progression
Sun, T., & Zhang, J. (2021) · The Journal of Biochemistry · doi:10.1093/jb/mvab088 · Cited by 23 · see citing works
Cooperative binding promotes demand-driven recruitment of AnxA8 to cholesterol-containing membranes
Heitzig, N., Kühnl, A., Grill, D., Ludewig, K., Schloer, S., Galla, H., Grewal, T., Gerke, V., & Rescher, U. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2018.01.001 · Cited by 23 · see citing works
DAMPs and influenza virus infection in ageing
Samy, R. P., & Lim, L. H. K. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.07.005 · Cited by 22 · see citing works
Proteomic analysis identifies differentially expressed proteins after red propolis treatment in Hep-2 cells
Frozza, C. O. D. S., Ribeiro, T. D. S., Gambato, G., Menti, C., Moura, S., Pinto, P. M., Staats, C. C., Padilha, F. F., Begnini, K. R., de Leon, P. M. M., et al. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.11.003 · Cited by 22 · see citing works
Annexin A5 overexpression might suppress proliferation and metastasis of human uterine cervical carcinoma cells1
Li, X., Ma, W., Wang, X., Ci, Y., & Zhao, Y. (2018) · Cancer Biomarkers · doi:10.3233/cbm-171040 · Cited by 22 · see citing works
Angiostrongylus cantonensis Galectin-1 interacts with Annexin A2 to impair the viability of macrophages via activating JNK pathway
Shi, X., Xiao, M., Xie, Z., Shi, Q., Zhang, Y., Leavenworth, J. W., Yan, B., & Huang, H. (2020) · Parasites & Vectors · doi:10.1186/s13071-020-04038-w · Cited by 21 · see citing works
Molecular Understanding of Growth Inhibitory Effect from Irradiated to Bystander Tumor Cells in Mouse Fibrosarcoma Tumor Model
Desai, S., Nishad, S., Yadav, H. D., Shetake, N. G., Balla, M. M. S., Kumar, A., Ray, P., Ghosh, A., & Pandey, B. N. (2016) · PLoS ONE · doi:10.1371/journal.pone.0161662 · Cited by 21 · see citing works
Clues from the intestinal mucus proteome of Atlantic salmon to counter inflammation
Kiron, V., Purushothaman, K., Fernandes, J. M. O., Sørensen, M., Vasanth, G. K., Lin, Q., Lin, Q., Lim, T. K., Dahle, D., Dias, J. P., et al. (2022) · Journal of Proteomics · doi:10.1016/j.jprot.2022.104487 · Cited by 20 · see citing works
Interactions between plant lipid-binding proteins and their ligands
Guo, Z.-H., Lung, S.-C., Hamdan, M. F., & Chye, M.-L. (2022) · Progress in Lipid Research · doi:10.1016/j.plipres.2022.101156 · Cited by 20 · see citing works
N-dihydrogalactochitosan-supported tumor control by photothermal therapy and photothermal therapy-generated vaccine
Korbelik, M., Banáth, J. P., Zhang, W., Hode, T., Lam, S. S. K., Gallagher, P., Zhao, J., Zeng, H., & Chen, W. R. (2020) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2020.111780 · Cited by 20 · see citing works
HDX-MS for Epitope Characterization of a Therapeutic ANTIBODY Candidate on the Calcium-Binding Protein Annexin-A1
Gramlich, M., Hays, H. C. W., Crichton, S. J., Kaiser, P. D., Heine, A., Schneiderhan‐Marra, N., Rothbauer, U., Stoll, D., Maier, S. M., & Zeck, A. (2021) · Antibodies · doi:10.3390/antib10010011 · Cited by 20 · see citing works
ANNEXIN A1: Roles in Placenta, Cell Survival, and Nucleus
de Sousa, S. O., dos Santos, M. R., Teixeira, S. C., Ferro, E. A. V., & Oliani, S. M. (2022) · Cells · doi:10.3390/cells11132057 · Cited by 19 · see citing works
Novel Platinum(II) and Platinum(IV) Antitumor Agents that Exhibit Potent Cytotoxicity and Selectivity
Khoury, A., Elias, E., Mehanna, S., Shebaby, W. N., Deo, K. M., Mansour, N., Khalil, C., Sayyed, K., Sakoff, J. A., Gilbert, J., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01310 · Cited by 19 · see citing works
Human Annexins A1, A2, and A8 as Potential Molecular Targets for Ni(II) Ions
Wezynfeld, N. E., Bossak‐Ahmad, K., Goch, W., Bonna, A., Bal, W., & Frączyk, T. (2014) · Chemical Research in Toxicology · doi:10.1021/tx500337w · Cited by 19 · see citing works
Plasma Membrane Protein Profiling in Beta‐Amyloid‐Treated Microglia Cell Line
Correani, V., Francesco, L. D., Mignogna, G., Fabrizi, C., Leone, S., Giorgi, A., Passeri, A., Casata, R., Fumagalli, L., Maras, B., et al. (2017) · PROTEOMICS · doi:10.1002/pmic.201600439 · Cited by 20 · see citing works
Quantitative methods to detect phospholipids at the oil-water interface
Perazzo, A., Gallier, S., Liuzzi, R., Guido, S., & Caserta, S. (2021) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2021.102392 · Cited by 19 · see citing works
Annexin Induces Cellular Uptake of Extracellular Vesicles and Delays Disease in Escherichia coli O157:H7 Infection
Tontanahal, A., Arvidsson, I., & Karpman, D. (2021) · Microorganisms · doi:10.3390/microorganisms9061143 · Cited by 19 · see citing works
Insights Into the Mechanisms of Brain Endothelial Erythrophagocytosis
Sun, J., Vyas, P. D., Mann, S., Paganini‐Hill, A., Nunes, A. C. F., Lau, W. L., Cribbs, D. H., Fisher, M., & Sumbria, R. K. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.672009 · Cited by 19 · see citing works
Annexin A5 stabilizes matrix vesicle-biomimetic lipid membranes: unravelling a new role of annexins in calcification
Ferreira, C. R., Cruz, M. A. E., Bolean, M., Andrilli, L. H. D. S., Millán, J. L., Ramos, A. P., Bottini, M., & Ciancaglini, P. (2023) · European Biophysics Journal · doi:10.1007/s00249-023-01687-4 · Cited by 18 · see citing works
Proteome of the Triatomine Digestive Tract: From Catalytic to Immune Pathways; Focusing on Annexin Expression
Gumiel, M., de Mattos, D. P., Vieira, C. S., Moraes, C. D. S., Moreira, C. J. D. C., Gonzalez, M. S., Teixeira‐Ferreira, A., Waghabi, M. C., Azambuja, P., & Carels, N. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.589435 · Cited by 18 · see citing works
Membrane repair triggered by cholesterol-dependent cytolysins is activated by mixed lineage kinases and MEK
Ray, S., Roth, R. A., & Keyel, P. A. (2022) · Science Advances · doi:10.1126/sciadv.abl6367 · Cited by 18 · see citing works
Structures of annexin A2-PS DNA complexes show dominance of hydrophobic interactions in phosphorothioate binding
Hyjek‐Składanowska, M., Anderson, B. A., Mykhaylyk, V. B., Orr, C. M., Wagner, A., Poznański, J. T., Skowronek, K. J., Seth, P. P., & Nowotny, M. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac774 · Cited by 18 · see citing works
The catalytic domains ofClostridium sordelliilethal toxin and related large clostridial glucosylating toxins specifically recognize the negatively charged phospholipids phosphatidylserine and phosphatidic acid
Chavez, C. V., Hoos, S., Haustant, M., Chenal, A., England, P., Blondel, A., Pauillac, S., Lacy, D. B., & Popoff, M. R. (2015) · Cellular Microbiology · doi:10.1111/cmi.12449 · Cited by 18 · see citing works
Sp1 promotes cell migration and invasion in oral squamous cell carcinoma by upregulating Annexin A2 transcription
Liu, X.-B., Wang, J., Li, K., & Fan, X.-N. (2019) · Molecular and Cellular Probes · doi:10.1016/j.mcp.2019.06.007 · Cited by 18 · see citing works
Anxa4 mediated airway progenitor cell migration promotes distal epithelial cell fate specification
Jiang, K., Tang, Z., Li, J., Wang, F., & Tang, N. (2018) · Scientific Reports · doi:10.1038/s41598-018-32494-z · Cited by 17 · see citing works
An alternative N-terminal fold of the intestine-specific annexin A13a induces dimerization and regulates membrane-binding
McCulloch, K. M., Yamakawa, I., Shifrin, D. A., McConnell, R. E., Foegeding, N. J., Singh, P. K., Mao, S., Tyska, M. J., & Iverson, T. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004571 · Cited by 17 · see citing works
Expression profiles of Annexin A1, formylated peptide receptors and cyclooxigenase-2 in gastroesophageal inflammations and neoplasias
Takaoka, R. T. C., Sertório, N. D., Magalini, L. P. J., Santos, L. M. D., Souza, H. R., Iyomasa-Pilon, M. M., Possebon, L., Costa, S. D. S., & Girol, A. P. (2017) · Pathology - Research and Practice · doi:10.1016/j.prp.2017.12.003 · Cited by 17 · see citing works

Authors: Lizarbe, M., Barrasa, J., Olmo, N., Gavilanes, F., & Turnay, J.
Affiliations: Universidad Complutense de Madrid (ES)
Corresponding author: Turnay, Javier
ORCID: Lizarbe, María
Olmo, Nieves
Gavilanes, Francisco
Turnay, Javier
Venue: International Journal of Molecular Sciences
Publisher: MDPI AG
Published: 2013-01-28
Volume: 14
Issue: 2
Pages: 2652-2683
ISSN: 1422-0067 (ISSN-L)
DOI: 10.3390/ijms14022652
PMC: PMC3588008
OpenAlex: W2088080018
Cited by: 234
References: 173
Citations by year: 2026: 10 · 2025: 13 · 2024: 14 · 2023: 16 · 2022: 27 · 2021: 29 · 2020: 27 · 2019: 21 · 2018: 18 · 2017: 14 · 2016: 16 · 2015: 13 · 2014: 11 · 2013: 5
FWCI: 6.72
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/3.0/ (vor)
Locations: International Journal of Molecular Sciences (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Library Open Repository (Universidad Complutense Madrid) (submittedVersion, cc-by)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: Ministerio de Ciencia e Innovación (BFU2008-04758)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
Keywords: annexins, phospholipid binding, calcium-dependent membrane binding, anionic phospholipids, phosphatidylserine, membrane trafficking, ion channel modulation, anti-inflammatory activity, anticoagulant activity, protein superfamilies

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Annexin-Phospholipid Interactions. Functional Implications

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks