Annexin II tetramer: structure and function

A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion

Söllner, T., Bennett, M. K., Whiteheart, S. W., Scheller, R. H., & Rothman, J. E. (1993) · Cell · doi:10.1016/0092-8674(93)90376-2 · Cited by 1,896

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 1,099

Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells

Sargiacomo, M., Sudol, M., Tang, Z., & Lisanti, M. (1993) · The Journal of cell biology · doi:10.1083/jcb.122.4.789 · Cited by 953

The molecular machinery for secretion is conserved from yeast to neurons.

Bennett, M. K., & Scheller, R. H. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.7.2559 · Cited by 650

The Annexins and Exocytosis

Creutz, C. E. (1992) · Science · doi:10.1126/science.1439804 · Cited by 548

Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; calcium-dependent binding to non-erythroid spectrin and F-actin.

Gerke, V., & Weber, K. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb01789.x · Cited by 539

Aggregation of chromaffin granules by calpactin at micromolar levels of calcium

Drust, D. S., & Creutz, C. E. (1988) · Nature · doi:10.1038/331088a0 · Cited by 437

Calcium requirements for secretion in bovine chromaffin cells.

Augustine, G. J., & Neher, E. (1992) · The Journal of Physiology · doi:10.1113/jphysiol.1992.sp019126 · Cited by 414

The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes.

Huber, R., Römisch, J., & Paques, E. P. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07605.x · Cited by 407

Protein-Protein Interactions Contributing to the Specificity of Intracellular Vesicular Trafficking

Calakos, N., Bennett, M. K., Peterson, K. E., & Scheller, R. H. (1994) · Science · doi:10.1126/science.8108733 · Cited by 399

Cancer metastasis: tumor cell and host organ properties important in metastasis to specific secondary sites

Nicolson, G. L. (1988) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(88)90010-8 · Cited by 399

Calcium-dependent phospholipid- (and membrane-) binding proteins

Klee, C. B. (1988) · Biochemistry · doi:10.1021/bi00418a001 · Cited by 374

Binding of annexin V/placental anticoagulant protein I to platelets. Evidence for phosphatidylserine exposure in the procoagulant response of activated platelets.

Thiagarajan, P., & Tait, J. F. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)38177-8 · Cited by 366

The Cellular Basis of Site-Specific Tumor Metastasis

Flier, J. S., Underhill, L. H., & Zetter, B. R. (1990) · New England Journal of Medicine · doi:10.1056/nejm199003013220907 · Cited by 349

An endothelial cell receptor for plasminogen/tissue plasminogen activator (t-PA). II. Annexin II-mediated enhancement of t-PA-dependent plasminogen activation.

Cesarman, G. M., Guevara, C. A., & Hajjar, K. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31948-8 · Cited by 341

Catecholamine secretion from digitonin-treated adrenal medullary chromaffin cells.

Dunn, L. A., & Holz, R. W. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32526-2 · Cited by 333

A role for calpactin in calcium-dependent exocytosis in adrenal chromaffin cells

Ali, S. M., Geisow, M. J., & Burgoyne, R. D. (1989) · Nature · doi:10.1038/340313a0 · Cited by 321

A consensus amino-acid sequence repeat in Torpedo and mammalian Ca2+-dependent membrane-binding proteins

Geisow, M. J., Fritsche, U., Hexham, J. M., Dash, B., & Johnson, T. (1986) · Nature · doi:10.1038/320636a0 · Cited by 313

Characterization of Ca2+-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins

Blackwood, R. A., & Ernst, J. D. (1990) · Biochemical Journal · doi:10.1042/bj2660195 · Cited by 290

The annexin family of calcium-binding proteins

Burgoyne, R. D., & Geisow, M. J. (1989) · Cell Calcium · doi:10.1016/0143-4160(89)90038-9 · Cited by 284

Transformation by Rous sarcoma virus: effects of src gene expression on the synthesis and phosphorylation of cellular polypeptides.

Radke, K., & Martin, G. S. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.10.5212 · Cited by 278

SNAP family of NSF attachment proteins includes a brain-specific isoform

Whiteheart, S. W., Griff, I. C., Brunner, M., Clary, D. O., Mayer, T., Buhrow, S. A., & Rothman, J. E. (1993) · Nature · doi:10.1038/362353a0 · Cited by 275

Annexin II is a major component of fusogenic endosomal vesicles.

Emans, N., Gorvel, J. P., Walter, C., Gerke, V, Kellner, R., Griffiths, G., & Gruenberg, J. (1993) · The Journal of cell biology · doi:10.1083/jcb.120.6.1357 · Cited by 269

Amino-terminal sequence of p36 and associated p10: identification of the site of tyrosine phosphorylation and homology with S-100.

Glenney, J. R., & Tack, B. F. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.23.7884 · Cited by 263

Phospholipid-dependent Ca2+ binding by the 36-kDa tyrosine kinase substrate (calpactin) and its 33-kDa core.

Glenney, J. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38382-5 · Cited by 261

Protein terminology tangle

CRUMPTON, M. J., & DEDMAN, J. R. (1990) · Nature · doi:10.1038/345212a0 · Cited by 256

Crystal and molecular structure of human annexin V after refinement

Huber, R., Berendes, R., Burger, A., Schneider, M., Karshikov, A., Luecke, H., Römisch, J., & Paques, E. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90984-r · Cited by 246

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., & Paques, E.-P. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)81428-q · Cited by 243

Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C.

Chung, C. Y., & Erickson, H. P. (1994) · The Journal of cell biology · doi:10.1083/jcb.126.2.539 · Cited by 232

Clustering of lipid-bound annexin V may explain its anticoagulant effect.

Andree, H. A., Stuart, M. C., Hermens, W. T., Reutelingsperger, C. P., Hemker, H. C., Frederik, P. M., & Willems, G. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37128-5 · Cited by 227

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

Calcium-activated endonexin II forms calcium channels across acidic phospholipid bilayer membranes.

Rojas, E., Pollard, H. B., Haigler, H. T., Parra, C., & Burns, A. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)45347-6 · Cited by 212

The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo.

Gould, K. L., Woodgett, J. R., Isacke, C. M., & Hunter, T. (1986) · Molecular and Cellular Biology · doi:10.1128/mcb.6.7.2738 · Cited by 207

Calcium-dependent conformational changes in the 36-kDa subunit of intestinal protein I related to the cellular 36-kDa target of Rous sarcoma virus tyrosine kinase.

Gerke, V, & Weber, K. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89649-1 · Cited by 200

The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C.

Sarafian, T., Pradel, L. A., Henry, J. P., Aunis, D., & Bader, M. F. (1991) · The Journal of cell biology · doi:10.1083/jcb.114.6.1135 · Cited by 196

p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix.

Johnsson, N., Marriott, G., & Weber, K. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03089.x · Cited by 195

Rat Annexin V Crystal Structure: Ca 2+ -Induced Conformational Changes

Concha, N. O., Head, J. F., Kaetzel, M. A., Dedman, J. R., & Seaton, B. A. (1993) · Science · doi:10.1126/science.8362244 · Cited by 192

Two related but distinct forms of the Mr 36,000 tyrosine kinase substrate (calpactin) that interact with phospholipid and actin in a Ca2+-dependent manner.

Glenney, J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.12.4258 · Cited by 191

Regulation of calpactin I phospholipid binding by calpactin I light-chain binding and phosphorylation by p60v-src

Powell, M. A., & Glenney, J. R. (1987) · Biochemical Journal · doi:10.1042/bj2470321 · Cited by 184

Conformational change and localization of calpactin I complex involved in exocytosis as revealed by quick-freeze, deep-etch electron microscopy and immunocytochemistry.

Nakata, T., Sobue, K., & Hirokawa, N. (1990) · The Journal of cell biology · doi:10.1083/jcb.110.1.13 · Cited by 183

Characterization of the chromobindins. Soluble proteins that bind to the chromaffin granule membrane in the presence of Ca2+.

Creutz, C. E., Dowling, L. G., Sando, J. J., Villar-Palasi, C., Whipple, J. H., & Zaks, W. J. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43914-7 · Cited by 182

Identification of chromaffin granule-binding proteins. Relationship of the chromobindins to calelectrin, synhibin, and the tyrosine kinase substrates p35 and p36.

Creutz, C. E., Zaks, W. J., Hamman, H. C., Crane, S., Martin, W. H., Gould, K. L., Oddie, K. M., & Parsons, S. J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75719-6 · Cited by 173

The tight association of the tyrosine kinase substrate annexin ii with the submembranous cytoskeleton depends on intact p11- and Ca2+-binding sites

Thiel, C., Osborn, M., & Gerke, V. (1992) · Journal of Cell Science · doi:10.1242/jcs.103.3.733 · Cited by 172

The calpactin light chain is tightly linked to the cytoskeletal form of calpactin I: studies using monoclonal antibodies to calpactin subunits.

Zokas, L., & Glenney, J. R. (1987) · The Journal of cell biology · doi:10.1083/jcb.105.5.2111 · Cited by 169

Crystal structure of human annexin I at 2.5 Å resolution

Weng, X., Luecke, H., Song, I. S., Kang, D. S., Kim, S., & Huber, R. (1993) · Protein Science · doi:10.1002/pro.5560020317 · Cited by 168

Collagen-binding proteins in collagenase-released matrix vesicles from cartilage. Interaction between matrix vesicle proteins and different types of collagen.

Wu, L. N., Genge, B. R., Lloyd, G. C., & Wuthier, R. E. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35301-2 · Cited by 162

Detection of phosphotyrosine-containing 34,000-dalton protein in the framework of cells transformed with Rous sarcoma virus.

Cheng, Y. S., & Chen, L. B. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.4.2388 · Cited by 149

Nerve growth factor induces the genes for two proteins related to a family of calcium-binding proteins in PC12 cells.

Masiakowski, P., & Shooter, E. M. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.4.1277 · Cited by 143

The 34 kd pp60src substrate is located at the inner face of the plasma membrane

Greenberg, M. E., & Edelman, G. M. (1983) · Cell · doi:10.1016/0092-8674(83)90019-3 · Cited by 142

Common domain structure of Ca2+ and lipid‐binding proteins

Geisow, M. J. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)81445-4 · Cited by 138

Stimulus response coupling : the role of intracellular calcium-binding proteins

Smith, V. L., & Dedman, J. R. (1990) · CRC Press eBooks · Cited by 135

Loss of proteins from digitonin-permeabilized adrenal chromaffin cells essential for exocytosis.

Sarafian, T., Aunis, D., & Bader, M. F. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)49307-6 · Cited by 124

Ca2+-activated synexin forms highly selective, voltage-gated Ca2+ channels in phosphatidylserine bilayer membranes.

Pollard, H. B., & Rojas, E. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.9.2974 · Cited by 123

Biosynthesis, secretion and extracellular localization of anchorin CII, a collagen‐binding protein of the calpactin family.

Pfäffle, M., Ruggiero, F., Hofmann, H., Fernández, M. P., Selmin, O. I., Yamada, Y., Garrone, R., & von der Mark, K. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03077.x · Cited by 121

The Crystal Structure of a New High-calcium Form of Annexin V

Santos, J. S. O., Renouard, M., & Lewit‐Bentley, A. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1627 · Cited by 119

Functionally distinct serine phosphorylation sites of p36, the cellular substrate of retroviral protein kinase; differential inhibition of reassociation with p11.

Johnsson, N., Van, P. N., Söling, H., & Weber, K. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04669.x · Cited by 117

Alterations of annexin expression in pathological neuronal and glial reactions. Immunohistochemical localization of annexins I, II (p36 and p11 subunits), IV, and VI in the human hippocampus.

Eberhard, D. A., Brown, M. D., & VandenBerg, S. R. (1994) · PubMed · Cited by 115

SNAP‐25 is present in a SNARE complex in adrenal chromaffin cells

Roth, D., & Burgoyne, R. D. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00833-7 · Cited by 111

Calcium-dependent regulation of actin filament bundling by lipocortin-85.

Ikebuchi, N. W., & Waisman, D. M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39780-7 · Cited by 109

Extracellular annexin II is associated with divalent cation‐dependent tumor cell–endothelial cell adhesion of metastatic RAW117 large‐cell lymphoma cells

Tressler, R., Updyke, T. V., Yeatman, T. J., & Nicolson, G. L. (1993) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240530311 · Cited by 108

A multiprotein form of DNA polymerase alpha from HeLa cells. Resolution of its associated catalytic activities.

Vishwanatha, J. K., Coughlin, S. A., Wesolowski-Owen, M., et al. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84608-2 · Cited by 106

The submembranous location of p11 and its interaction with the p36 substrate of pp60 src kinase in situ

Osborn, M., Johnsson, N., Wehland, J., & Weber, K. K. (1988) · Experimental Cell Research · doi:10.1016/0014-4827(88)90257-1 · Cited by 104

Structure of soluble and membrane-bound human annexin V

Brisson, A. R., Mosser, G., & Huber, R. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90002-n · Cited by 100

Expression of annexins on the surfaces of non-metastatic and metastatic human and rodent tumor cells

Yeatman, T. J., Updyke, T. V., Kaetzel, M. A., Dedman, J. R., & Nicolson, G. L. (1993) · Clinical & Experimental Metastasis · doi:10.1007/bf00880064 · Cited by 99

Phosphorylation of annexin II tetramer by protein kinase C inhibits aggregation of lipid vesicles by the protein.

Johnstone, S. A., Hubaishy, I., & Waisman, D. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35704-1 · Cited by 98

The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is part of the primer recognition protein complex that interacts with DNA polymerase alpha.

Jindal, H. K., Chaney, W. G., Anderson, C. W., Davis, R. G., & Vishwanatha, J. K. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67770-7 · Cited by 92

cDNA sequence and tissue distribution of the mRNA for bovine and murine p11, the S100-related light chain of the protein-tyrosine kinase substrate p36 (calpactin I).

Saris, C. J. M., Kristensen, T., D’Eustachio, P., Hicks, L., Noonan, D. J., Hunter, T. R., & Tack, B. F. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61015-4 · Cited by 92

Annexins in membrane traffic

Grüenberg, J., & Emans, N. (1993) · Trends in Cell Biology · doi:10.1016/0962-8924(93)90116-i · Cited by 92

In vitro protein kinase C phosphorylation sites of placental lipocortin

Schlaepfer, D. D., & Haigler, H. T. (1988) · Biochemistry · doi:10.1021/bi00412a008 · Cited by 84

Modulation of annexin II tetramer by tyrosine phosphorylation

Hubaishy, I., Jones, P. G., Bjorge, J. D., Bellagamba, C., Fitzpatrick, S., Fujita, D. J., & Waisman, D. M. (1995) · Biochemistry · doi:10.1021/bi00044a031 · Cited by 84

Calcium channel and membrane fusion activity of synexin and other members of the Annexin gene family

Pollard, H. B., Guy, H. R., Arispe, N. J., de la Fuente, M., Lee, G., Rojas, E., Pollard, J. R., Srivastava, M., Keck, Z., & Merezhinskaya, N. (1992) · Biophysical Journal · doi:10.1016/s0006-3495(92)81764-2 · Cited by 80

Phospholipid binding of antiphospholipid antibodies and placental anticoagulant protein

Sammaritano, L. R., Gharavi, A. E., Soberano, C., Levy, R. A., & Lockshin, M. D. (1992) · Journal of Clinical Immunology · doi:10.1007/bf00918270 · Cited by 78

Calpactin in exocytosis?

Burgoyne, R. D. (1988) · Nature · doi:10.1038/331020a0 · Cited by 75

Purification and characterization of proteolytic fragments of lipocortin I that inhibit phospholipase A2.

Huang, K., McGray, P., Mattaliano, R. J., Burne, C., Chow, E. P., Sinclair, L. K., & Pepinsky, R. B. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47614-4 · Cited by 74

Purification and characterization of annexin proteins from bovine lung

Khanna, N., Helwig, E. D., Ikebuchi, N. W., Fitzpatrick, S., Bajwa, R., & Waisman, D. M. (1990) · Biochemistry · doi:10.1021/bi00472a015 · Cited by 66

Annexin II contains two types of Ca2+-binding sites

Jost, M., Weber, K., & Gerke, V. (1994) · Biochemical Journal · doi:10.1042/bj2980553 · Cited by 66

Identification of a key domain in annexin and 14‐3‐3 proteins that stimulate calcium‐dependent exocytosis in permeabilized adrenal chromaffin cells

Roth, D., Morgan, A., & Burgoyne, R. D. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80587-k · Cited by 64

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

Functional identity of a primer recognition protein as phosphoglycerate kinase.

Jindal, H. K., & Vishwanatha, J. K. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39179-3 · Cited by 62

Calcium influx through annexin V ion channels into large unilamellar vesicles measured with fura‐2

Berendes, R., Bürger, A., Voges, D., Demange, P., & Huber, R. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81507-v · Cited by 61

The growth-regulated gene 1B6 is identified as the heavy chain of calpactin I

Keutzer, J. C., & Hirschhorn, R. R. (1990) · Experimental Cell Research · doi:10.1016/0014-4827(90)90291-h · Cited by 61

A key role for a 145-kDa cytosolic protein in the stimulation of Ca(2+)-dependent secretion by protein kinase C.

Nishizaki, T., Walent, J. H., Kowalchyk, J. A., & Martin, T. F. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35932-5 · Cited by 59

Autoantibodies to the centrosome (centriole) react with determinants present in the glycolytic enzyme enolase

Rattner, J. B., Martin, L., Waisman, D. M., et al. (1991) · The Journal of Immunology · doi:10.4049/jimmunol.146.7.2341 · Cited by 56

Involvement of annexin II in DNA replication: evidence from cell-free extracts of Xenopus eggs

Vishwanatha, J. K., & Kumble, S. (1993) · Journal of Cell Science · doi:10.1242/jcs.105.2.533 · Cited by 56

Differentiation of HL‐60 cells is associated with an increase in the 35‐kDa protein lipocortin I

William, F., Mroczkowski, B., Cohen, S., & Kraft, A. S. (1988) · Journal of Cellular Physiology · doi:10.1002/jcp.1041370303 · Cited by 56

Structural and Electrophysiological Analysis of Annexin V Mutants

Bürger, A., Voges, D., Demange, P., Ruíz-Pérez, C., Huber, R., & Berendes, R. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1249 · Cited by 55

Protein kinase C activation by phorbol esters induces chromaffin cell cortical filamentous actin disassembly and increases the initial rate of exocytosis in response to nicotinic receptor stimulation

Vitale, M. L., Castillo, A. R. D., & Trifaró, J. M. (1992) · Neuroscience · doi:10.1016/0306-4522(92)90330-5 · Cited by 55

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

Exocytosis in adrenal chromaffin cells.

Burgoyne, R. D., Morgan, A., Robinson, I. M., Pender, N., & Cheek, T. R. (1993) · Europe PMC (PubMed Central) · Cited by 53

Involvement of annexin I and annexin II in hepatocyte proliferation: Can annexins I and II be markers for proliferative hepatocytes?

Masaki, T., Tokuda, M., Fujimura, T., Ohnishi, M., Tai, Y., Miyamoto, K., Itano, T., Matsui, H., Watanabe, S., Sogawa, K.-I., et al. (1994) · Hepatology · doi:10.1002/hep.1840200224 · Cited by 51

Quick-freeze, deep-etch visualization of exocytosis in anterior pituitary secretory cells: localization and possible roles of actin and annexin II

Senda, T., Okabe, T., Matsuda, M., & Fujita, H. (1994) · Cell and Tissue Research · doi:10.1007/bf00303080 · Cited by 48

Phosphorylation and dephosphorylation of chromaffin cell proteins in response to stimulation

Coˆté, A., Doucet, J.-P., & Trifaró, J. M. (1986) · Neuroscience · doi:10.1016/0306-4522(86)90286-1 · Cited by 46

The stimulatory effect of calpactin (annexin II) on calcium-dependent exocytosis in chromaffin cells: Requirement for both the N-terminal and core domains of p36 and ATP

Ali, S. M., & Burgoyne, R. D. (1990) · Cellular Signalling · doi:10.1016/0898-6568(90)90054-e · Cited by 46

Demonstration of an endocrine signaling circuit for insulin in the sponge Geodia cydonium.

Robitzki, A. A., Schröder, H. C., Ugarković, Đ., et al. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08439.x · Cited by 44

Synaptic vesicle proteins and regulated exocytosis

Elferink, L. A., & Scheller, R. H. (1993) · Journal of Cell Science · doi:10.1242/jcs.1993.supplement_17.11 · Cited by 42

Synaptic vesicle proteins in exocytosis: what do we know?

Walch-Solimena, C., Jahn, R., & Südhof, T. C. (1993) · Current Opinion in Neurobiology · doi:10.1016/0959-4388(93)90125-i · Cited by 40

Immunocytochemical detection of extracellular annexin II in cultured human skin keratinocytes and isolation of annexin II isoforms enriched in the extracellular pool

Ma, A. S. P., Bell, D. J., Mittal, A., & Harrison, H. H. (1994) · Journal of Cell Science · doi:10.1242/jcs.107.7.1973 · Cited by 40

Protein kinase C and clostridial neurotoxins affect discrete and related steps in the secretory pathway

Bittner, M. A., & Holz, R. W. (1993) · Cellular and Molecular Neurobiology · doi:10.1007/bf00711564 · Cited by 38

Enolase is present at the centrosome of HeLa cells

Johnstone, S. A., Waisman, D. M., & Rattner, J. B. (1992) · Experimental Cell Research · doi:10.1016/0014-4827(92)90099-t · Cited by 34

Inhibition of Human Skin Phospholipase A2 by “Lipocortins” Is an Indirect Effect of Substrate/Lipocortin Interaction

Bastian, B. C., Sellert, C., Seekamp, A., Römisch, J., Pâques, E.-P., & Bröcker, E. ‐. (1993) · Journal of Investigative Dermatology · doi:10.1111/1523-1747.ep12365541 · Cited by 30

Carbohydrate-binding proteins in bovine kidney have consensus amino acid sequences of annexin family proteins.

Kojima, K., Ogawa, H. K., Seno, N., Yamamoto, K., Irimura, T., Osawa, T., & Matsumoto, I. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36715-8 · Cited by 27

Loss and Ca2+‐Dependent Retention of Scinderin in Digitonin‐Permeabilized Chromaffin Cells: Correlation with Ca2+‐Evoked Catecholamine Release

Vitale, M. L., Castillo, A. R. D., & Trifaró, J. M. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb11003.x · Cited by 26

Modulation of pp60c‐src tyrosine kinase activity during secretion in stimulated bovine adrenal chromaffin cells

Oddie, K. M., Litz, J., Balserak, J. C., Payne, D. M., Creutz, C. E., & Parson, S. J. (1989) · Journal of Neuroscience Research · doi:10.1002/jnr.490240107 · Cited by 26

Annexin V-crystal structure and its implications on function.

Huber, R., Berendes, R., Bürger, A., Luecke, H., & Karshikov, A. (1992) · PubMed · Cited by 25

Calpactin‐depleted cytosolic proteins restore Ca2+‐dependent secretion to digitonin‐permeabilized bovine chromaffin cells

Wu, Y. N., & Wagner, P. D. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80476-j · Cited by 24

Annexins Possess Functionally Distinguishable Ca2+ and Phospholipid Binding Domains

Ernst, J. D., Mall, A., & Chew, G. K. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1531 · Cited by 24

Butanol‐extractable and detergent‐solubilized cell surface components from murine large cell lymphoma cells associated with adhesion to organ microvessel endothelial cells

Tressler, R., & Nicolson, G. L. (1992) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240480208 · Cited by 23

Changes in actin and actin-binding proteins during the differentiation of HL-60 leukemia cells.

Leung, M., Lin, T. S., & Sartorelli, A. C. (1992) · PubMed · Cited by 22

In vitro modulation of filament bundling in f-actin and keratins by annexin II and calcium

Ma, A. S. P., Bystol, M. E., & Tranvan, A. (1994) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/bf02631454 · Cited by 17

Characterization of Proteins That Regulate Calcium‐dependent Exocytosis in Adrenal Chromaffin Cells

Burgoyne, R. D., Morgan, A., & Roth, D. (1994) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1994.tb26640.x · Cited by 14

Reconstitution of transmitter secretion

Alder, J., & Poo, M. (1993) · Current Opinion in Neurobiology · doi:10.1016/0959-4388(93)90124-h · Cited by 4

Annexins: From Structure to Function

Gerke, V., & Moss, S. E. (2002) · Physiological Reviews · doi:10.1152/physrev.00030.2001 · Cited by 2,029

S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles

Donato, R. (2001) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00046-2 · Cited by 1,580

An immune response manifested by the common occurrence of annexins I and II autoantibodies and high circulating levels of IL-6 in lung cancer

Brichory, F. M., Misek, D. E., Yim, A.-M., Krause, M. C., Giordano, T. J., Beer, D. G., & Hanash, S. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171320598 · Cited by 353

Annexin A2 is a natural extrahepatic inhibitor of the PCSK9-induced LDL receptor degradation

Seidah, N. G., Poirier, S., Denis, M., Parker, R., Miao, B., Mapelli, C., Prat, A., Wassef, H., Davignon, J., Hajjar, K. A., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041865 · Cited by 117

Co‐localization of the neonatal Fcγ receptor and IgG in human placental term syncytiotrophoblasts

Kristoffersen, E. K., & Matre, R. (1996) · European Journal of Immunology · doi:10.1002/eji.1830260741 · Cited by 90