Lipocalins - a family portrait

The lipocalin protein family: structure and function

FLOWER, D. R. (1996) · Biochemical Journal · doi:10.1042/bj3180001 · Cited by 1,679 · see citing works

The lipocalin protein family: structural and sequence overview

Flower, D. R., North, A. C. T., & Sansom, C. E. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00148-5 · Cited by 868 · see citing works

An Iron Delivery Pathway Mediated by a Lipocalin

Yang, J., Goetz, D., Li, J.-Y., Wang, W., Mori, K., Setlik, D., Du, T., Erdjument-Bromage, H., Tempst, P., Strong, R., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00710-4 · Cited by 651 · see citing works

Molecular identification of zeaxanthin epoxidase of Nicotiana plumbaginifolia, a gene involved in abscisic acid biosynthesis and corresponding to the ABA locus of Arabidopsis thaliana.

Marín, E., Nussaume, L., Quesada, A., Gonneau, M., Sotta, B., Hugueney, P., Frey, A., & Marion‐Poll, A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00589.x · Cited by 550 · see citing works

The three‐dimensional structure of retinol‐binding protein.

Newcomer, M. E., Jones, T. A., Aqvist, J., Sundelin, J., Eriksson, U., Rask, L., & Peterson, P. A. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb01995.x · Cited by 405 · see citing works

The core lipocalin, bovine β-lactoglobulin

Sawyer, L., & Kontopidis, G. A. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00160-6 · Cited by 380 · see citing works

A Model for the Denaturation and Aggregation of β‐Lactoglobulin

Roefs, S. P. F. M., & de Kruif, C. G. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.00883.x · Cited by 378 · see citing works

Biochemistry of the violaxanthin cycle in higher plants

Yamamoto, H. Y. (1979) · Pure and Applied Chemistry · doi:10.1351/pac197951030639 · Cited by 372 · see citing works

Structure and sequence relationships in the lipocalins and related proteins

Flower, D. R., North, A. C. T., & Attwood, T. K. (1993) · Protein Science · doi:10.1002/pro.5560020507 · Cited by 342 · see citing works

Biochemical, structural, genetic, physiological, and pathophysiological features of lipocalin-type prostaglandin D synthase

Urade, Y., & Hayaishi, O. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00161-8 · Cited by 337 · see citing works

A Novel Human Apolipoprotein (apoM)

Xu, N., & Dahlbäck, B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.44.31286 · Cited by 336 · see citing works

The Epididymis: From Molecules to Clinical Practice

(2002) · Springer eBooks · doi:10.1007/978-1-4615-0679-9 · Cited by 321 · see citing works

Tick Histamine-Binding Proteins

Paesen, G. C., Adams, P. L., Harlos, K., Nuttall, P. A., & Stuart, D. I. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80359-7 · Cited by 310 · see citing works

β-Lactoglobulin Binds Palmitate within Its Central Cavity

Wu, S., Pérez, M. D., Puyol, P., & Sawyer, L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.1.170 · Cited by 301 · see citing works

Lichtbedingte pH-Erniedrigung in einem Chloroplasten-Kompartiment als Ursache der enzymatischen Violaxanthin-? Zeaxanthin-Umwandlung; Beziehungen zur Photophosphorylierung

Hager, A. (1969) · Planta · doi:10.1007/bf00385028 · Cited by 282 · see citing works

Lipocalins: unity in diversity

Åkerström, B., Flower, D. R., & Salier, J. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00137-0 · Cited by 270 · see citing works

The Ligand-binding Site of Bovine β-Lactoglobulin: Evidence for a Function?

Kontopidis, G. A., Holt, C., & Sawyer, L. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00017-7 · Cited by 264 · see citing works

Purification and characterization of rat brain prostaglandin D synthetase.

Urade, Y., Fujimoto, N., & Hayaishi, O. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38889-0 · Cited by 243 · see citing works

Evidence that introns arose at proto‐splice sites.

Dibb, N. J., & Newman, A. J. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03609.x · Cited by 242 · see citing works

A 25 kDa α2‐microglobulin‐related protein is a component of the 125 kDa form of human gelatinase

Triebel, S., Bläser, J., Reinke, H., & Tschesche, H. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81511-j · Cited by 229 · see citing works

The effects of dithiothreitol on violaxanthin de-epoxidation and absorbance changes in the 500-nm region

Yamamoto, H. Y., & Kamite, L. (1972) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(72)90182-x · Cited by 225 · see citing works

Violaxanthin de-epoxidase

Yamamoto, H. Y., & Higashi, R. (1978) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(78)90305-3 · Cited by 223 · see citing works

Cloning and expression of human apolipoprotein D cDNA.

Drayna, D. T., Fielding, C., McLean, J. W., Baer, B. W., Castro, G., Chen, E., COMSTOCK, L. J., Henzel, W. J., Kohr, W. J., & Rhee, L. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66599-8 · Cited by 218 · see citing works

The molecular basis of the coloration mechanism in lobster shell: β-Crustacyanin at 3.2-Å resolution

Cianci, M., Rizkallah, P. J., Ołczak, A., Raftery, J., Chayen, N. E., Zagalsky, P. F., & Helliwell, J. R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.152088999 · Cited by 209 · see citing works

Lipocalin-type and hematopoietic prostaglandin D synthases as a novel example of functional convergence.

Urade, Y., & Eguchi, N. (2002) · Prostaglandins & other lipid mediators · doi:10.1016/s0090-6980(02)00042-4 · Cited by 209 · see citing works

Lipocalin-type Prostaglandin D Synthase (β-Trace) Is a Newly Recognized Type of Retinoid Transporter

Tanaka, T., Urade, Y., Kimura, H., Eguchi, N., Nishikawa, A., & Hayaishi, O. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.25.15789 · Cited by 206 · see citing works

Prostaglandin synthases: recent developments and a novel hypothesis

Helliwell, R. J. A., Adams, L. F., & Mitchell, M. D. (2003) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/j.plefa.2003.04.002 · Cited by 203 · see citing works

Immunocalins: a lipocalin subfamily that modulates immune and inflammatory responses

Lögdberg, L., & Wester, L. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00164-3 · Cited by 201 · see citing works

Evidence of an Odorant-Binding Protein in the Human Olfactory Mucus: Location, Structural Characterization, and Odorant-Binding Properties

Briand, L. V., Eloit, C., Nespoulous, C., Bézirard, V., Huet, J., Henry, C., Blon, F., Trotier, D., & Pernollet, J. C. (2002) · Biochemistry · doi:10.1021/bi015916c · Cited by 196 · see citing works

Transport of iron and other transition metals into cells as revealed by a fluorescent probe

Breuer, W., Epsztejn, S., Milgram, P., & Cabantchik, I. Z. (1995) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1995.268.6.c1354 · Cited by 185 · see citing works

Increased Levels of Apolipoprotein D in Cerebrospinal Fluid and Hippocampus of Alzheimer's Patients

Terrisse, L., Poirier, J., Bertrand, P., Merched, A. J., Visvikis‐Siest, S., Siest, G., Milne, R. W., & Rassart, É. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71041643.x · Cited by 179 · see citing works

Plant lipocalins: violaxanthin de-epoxidase and zeaxanthin epoxidase

Hieber, A. D., Bugos, R. C., & Yamamoto, H. Y. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00141-2 · Cited by 171 · see citing works

Xanthophyll Biosynthesis

Bouvier, F., d’Harlingue, A., Hugueney, P., Marín, E., Marion‐Poll, A., & Camara, B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.46.28861 · Cited by 170 · see citing works

Purification and characterisation of an odorant‐binding protein from cow nasal tissue

Bignetti, E., Cavaggioni, A., Pelosi, P., Persaud, K. C., Sorbi, R. T., & Tirindelli, R. (1985) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1985.tb08916.x · Cited by 170 · see citing works

Regulation of violaxanthin de-epoxidase activity by pH and ascorbate concentration

Welinder, C., Arvidsson, P., Carlsson, M., & �kerlund, H.-E. (1995) · Photosynthesis Research · doi:10.1007/bf00032588 · Cited by 165 · see citing works

Purification, Partial Characterization, and Cloning of Nitric Oxide-carrying Heme Proteins (Nitrophorins) from Salivary Glands of the Blood-sucking Insect Rhodnius prolixus

Champagne, D. E., Nussenzveig, R., & Ribeiro, J. M. C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.15.8691 · Cited by 164 · see citing works

A Phylogenetic Analysis of the Lipocalin Protein Family

Ganfornina, M. D., Gutiérrez, G., Bastiani, M. J., & Diego, S. (2000) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a026224 · Cited by 159 · see citing works

Molecular cloning of violaxanthin de-epoxidase from romaine lettuce and expression in Escherichia coli.

Bugos, R. C., & Yamamoto, H. Y. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.13.6320 · Cited by 153 · see citing works

Nitrophorins and related antihemostatic lipocalins from Rhodnius prolixus and other blood-sucking arthropods

Montfort, W. R., Weichsel, A., & Andersen, J. F. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00165-5 · Cited by 152 · see citing works

A high affinity serotonin‐ and histamine‐binding lipocalin from tick saliva

Sangamnatdej, S., Paesen, G. C., Slovák, M., & Nuttall, P. A. (2002) · Insect Molecular Biology · doi:10.1046/j.0962-1075.2001.00311.x · Cited by 152 · see citing works

Crystal structures of a nitric oxide transport protein from a blood-sucking insect

Weichsel, A., Andersen, J. F., Champagne, D. E., Walker, F. A., & Montfort, W. R. (1998) · Nature Structural Biology · doi:10.1038/nsb0498-304 · Cited by 152 · see citing works

Xanthophyll Cycle Enzymes Are Members of the Lipocalin Family, the First Identified from Plants

Bugos, R. C., Hieber, A. D., & Yamamoto, H. Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15321 · Cited by 148 · see citing works

Complexes of porcine odorant binding protein with odorant molecules belonging to different chemical classes

Vincent, F., Spinelli, S., Ramoni, R., Grolli, S., Pelosi, P., Cambillau, C., & Tegoni, M. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3820 · Cited by 148 · see citing works

The hydrophobic proteome of mitochondrial membranes from Arabidopsis cell suspensions

Brugière, S., Kowalski, S., Ferro, M., Seigneurin‐Berny, D., Miras, S., Salvi, D., Ravanel, S., d'Hérin, P., Garin, J., Bourguignon, J., et al. (2004) · Phytochemistry · doi:10.1016/j.phytochem.2004.03.028 · Cited by 134 · see citing works

Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug

Fuentes‐Prior, P., Noeske‐Jungblut, C., Donner, P., Schleuning, W.-D. D., Huber, R., & Bode, W. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.22.11845 · Cited by 132 · see citing works

Violaxanthin De-Epoxidase (Purification of a 43-Kilodalton Lumenal Protein from Lettuce by Lipid-Affinity Precipitation with Monogalactosyldiacylglyceride)

Rockholm, D. C., & Yamamoto, H. Y. (1996) · PLANT PHYSIOLOGY · doi:10.1104/pp.110.2.697 · Cited by 120 · see citing works

Violaxanthin De-Epoxidase, the Xanthophyll Cycle Enzyme, Requires Lipid Inverted Hexagonal Structures for Its Activity

Latowski, D., Åkerlund, H., & Strzałka, K. (2004) · Biochemistry · doi:10.1021/bi049652g · Cited by 118 · see citing works

Multiple molecular recognition properties of the lipocalin protein family

Flower, D. R. (1995) · Journal of Molecular Recognition · doi:10.1002/jmr.300080304 · Cited by 118 · see citing works

A novel type of receptor protein, based on the lipocalin scaffold, with specificity for digoxigenin11Edited by R. Huber

Schlehuber, S., Beste, G., & Skerra, A. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3646 · Cited by 115 · see citing works

The bacterial lipocalins

Bishop, R. E. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00138-2 · Cited by 113 · see citing works

Interaction of Fatty Acids with β-Lactoglobulin and Albumin from Ruminant Milk1

Pérez, M. D., de Villegas, C. D., Sánchez, L., Aranda, P., Ena, J. M., & Calvo, M. (1989) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a122971 · Cited by 110 · see citing works

Role of Hexagonal Structure-Forming Lipids in Diadinoxanthin and Violaxanthin Solubilization and De-Epoxidation

Goss, R., Lohr, M., Latowski, D., Grzyb, J., Vieler, A., Wilhelm, C., & Strzałka, K. (2005) · Biochemistry · doi:10.1021/bi047464k · Cited by 110 · see citing works

Apolipoprotein D in the aging brain and in Alzheimer’s dementia

Kalman, K., McConathy, W., Araoz, C., Kasa, P., & Lacko, A. G. (2000) · Neurological Research · doi:10.1080/01616412.2000.11740678 · Cited by 107 · see citing works

Regulation of progesterone-binding breast cyst protein GCDFP-24 secretion by estrogens and androgens in human breast cancer cells: a new marker of steroid action in breast cancer.

SIMARD, J., DAUVOIS, S., HAAGENSEN, D. E., LÉVESQUE, C., MÉRAND, Y., & LABRIE, F. (1990) · Endocrinology · doi:10.1210/endo-126-6-3223 · Cited by 107 · see citing works

The odorant-binding proteins of Drosophila melanogaster : annotation and characterization of a divergent gene family

Graham, L. A., & Davies, P. L. (2002) · Gene · doi:10.1016/s0378-1119(02)00672-8 · Cited by 106 · see citing works

Perineuronal Oligodendrocytes Protect against Neuronal Apoptosis through the Production of Lipocalin-Type Prostaglandin D Synthase in a Genetic Demyelinating Model

Taniike, M., Mohri, I., Eguchi, N., Beuckmann, C., Suzuki, K., & Urade, Y. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-12-04885.2002 · Cited by 106 · see citing works

Biochemical perspectives on paralysis and other forms of toxicoses caused by ticks

Mans, B. J., Gothe, R., & Neitz, A. W. H. (2004) · Parasitology · doi:10.1017/s0031182003004670 · Cited by 105 · see citing works

Exon-Intron Structure and Evolution of the Lipocalin Gene Family

Sánchez, D. (2003) · Molecular Biology and Evolution · doi:10.1093/molbev/msg079 · Cited by 104 · see citing works

Is apolipoprotein D a mammalian bilin-binding protein?

Peitsch, M. C., & Boguski, M. S. (1990) · PubMed · Cited by 101 · see citing works

The Insect Attractant 1-Octen-3-ol Is the Natural Ligand of Bovine Odorant-binding Protein

Ramoni, R., Vincent, F., Grolli, S., Conti, V., Malosse, C., Boyer, F., Meillour, P. N., Spinelli, S., Cambillau, C., & Tegoni, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010368200 · Cited by 100 · see citing works

Kinetics of violaxanthin de‐epoxidation by violaxanthin de‐epoxidase, a xanthophyll cycle enzyme, is regulated by membrane fluidity in model lipid bilayers

Latowski, D., Kruk, J., Burda, K., Skrzynecka, M., Kostecka‐Gugała, A., & Strzałka, K. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03166.x · Cited by 98 · see citing works

The xanthophyll cycle of Mantoniella squamata converts violaxanthin into antheraxanthin but not to zeaxanthin: consequences for the mechanism of enhanced non-photochemical energy dissipation

Goss, R., Böhme, K., & Wilhelm, C. (1998) · Planta · doi:10.1007/s004250050364 · Cited by 97 · see citing works

The primary structure of the human retinol‐binding protein

Rask, L., Anundi, H., & Peterson, P. A. (1979) · FEBS Letters · doi:10.1016/0014-5793(79)81084-4 · Cited by 97 · see citing works

A structural model of the chitin-binding domain of cuticle proteins

Hamodrakas, S. J., Willis, J. H., & Iconomidou, V. A. (2002) · Insect Biochemistry and Molecular Biology · doi:10.1016/s0965-1748(02)00079-6 · Cited by 95 · see citing works

The xanthophyll cycle - molecular mechanism and physiological significance

Latowski, D., Grzyb, J., & Strzałka, K. (2004) · Acta Physiologiae Plantarum · doi:10.1007/s11738-004-0009-8 · Cited by 93 · see citing works

Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site‐directed mutagenesis

Duan, J., Dahlbäck, B., & Villoutreix, B. O. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02544-3 · Cited by 90 · see citing works

Role of conserved residues in structure and stability: Tryptophans of human serum retinol‐binding protein, a model for the lipocalin superfamily

Greene, L. H., Chrysina, E. D., IRONS, L. I., Papageorgiou, A. C., Acharya, K. R., & Brew, K. (2001) · Protein Science · doi:10.1110/ps.22901 · Cited by 88 · see citing works

Structure of human -acid glycoprotein and its high-affinity binding site

Kopecký, V., Ettrich, R. H., Hofbauerová, K., & Baumruk, V. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02765-1 · Cited by 86 · see citing works

Effect of β-lactoglobulin on the activity of pregastric lipase. A possible role for this protein in ruminant milk

Pérez, M. D., Sánchez, L., Aranda, P., Ena, J. M., Oria, R., & Calvo, M. (1992) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(92)90105-5 · Cited by 85 · see citing works

Identification of a conserved hydrophobic cluster in partially folded bovine β-lactoglobulin at pH 2

Ragona, L., Pusterla, F., Zetta, L., Monaco, H. L., & Molinari, H. (1997) · Folding and Design · doi:10.1016/s1359-0278(97)00039-4 · Cited by 84 · see citing works

Molecular and structural analyses of a novel temperature stress‐induced lipocalin from wheat and Arabidopsis

Charron, J.-B. F., Breton, G., Badawi, M. A., & Sarhan, F. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02606-6 · Cited by 82 · see citing works

Interaction of an acute phase reactant, alpha 1-acid glycoprotein (orosomucoid), with the lymphoid cell surface: a model for non-specific immune suppression.

Cheresh, D. A., Haynes, D. H., & Distasio, J. A. (1984) · PubMed · Cited by 78 · see citing works

Stationary Phase Expression of a Novel Escherichia coli Outer Membrane Lipoprotein and Its Relationship with Mammalian Apolipoprotein D

Bishop, R. E., Penfold, S. S., Frost, L. S., Höltje, J., & Weiner, J. H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.39.23097 · Cited by 76 · see citing works

Odorant Binding and Conformational Changes of a Rat Odorant-binding Protein

Nespoulous, C. (2004) · Chemical Senses · doi:10.1093/chemse/bjh017 · Cited by 74 · see citing works

Lazarillo, a new GPI-linked surface lipocalin, is restricted to a subset of neurons in the grasshopper embryo

Ganfornina, M. D., Sánchez, D., & Bastiani, M. J. (1995) · Development · doi:10.1242/dev.121.1.123 · Cited by 73 · see citing works

PREPARATION AND PROPERTIES OF AN ACID GLYCOPROTEIN PREPARED FROM HUMAN PLASMA

Schmid, K. (1950) · Journal of the American Chemical Society · doi:10.1021/ja01162a553 · Cited by 71 · see citing works

Altered apolipoprotein D expression in the brain of patients with Alzheimer disease

Belloir, B., Kövari, E., Surini, M., & Savioz, A. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.1054 · Cited by 70 · see citing works

Die Zusammenhänge zwischen lichtinduzierten Xanthophyll‐Umwandlungen und Hill‐Reaktion

Hager, A. (1966) · Berichte der Deutschen Botanischen Gesellschaft · doi:10.1111/j.1438-8677.1966.tb04063.x · Cited by 67 · see citing works

‘Anticalins’: a new class of engineered ligand-binding proteins with antibody-like properties

Skerra, A. (2001) · Reviews in Molecular Biotechnology · doi:10.1016/s1389-0352(01)00020-4 · Cited by 67 · see citing works

Crystal structures of bovine odorant‐binding protein in complex with odorant molecules

Vincent, F., Ramoni, R., Spinelli, S., Grolli, S., Tegoni, M., & Cambillau, C. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04315.x · Cited by 66 · see citing works

YodA from Escherichia coli is a metal-binding, lipocalin-like protein

David, G., Blondeau, K., Schiltz, M., Penel, S., & Lewit-Bentley, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304484200 · Cited by 63 · see citing works

Endonuclease activity in lipocalins

Yusifov, T., Abduragimov, A. R., Gasymov, O. K., & Glasgow, B. J. (2000) · Biochemical Journal · doi:10.1042/bj3470815 · Cited by 62 · see citing works

Control of domain swapping in bovine odorant-binding protein

Ramoni, R., Vincent, F., Ashcroft, A. E., Accornero, P., Grolli, S., VALENCIA, C., Tegoni, M., & Cambillau, C. (2002) · Biochemical Journal · doi:10.1042/bj20011631 · Cited by 62 · see citing works

IS APOLIPOPROTEIN D A MAMMALIAN BILIN-BINDING PROTEIN?

PEITSCH, M. C. ;. B. (1992) · ModelArchive SIB · doi:10.5452/ma-c1x8v · Cited by 59 · see citing works

Immunohistochemical study of distribution of apolipoproteins E and D in human cerebral β amyloid deposits

Navarro, A., del Valle, E., Astudillo, A., del Rey, C. G., & Tolivia, J. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(03)00315-7 · Cited by 58 · see citing works

Functional Characterization of Olfactory Binding Proteins for Appeasing Compounds and Molecular Cloning in the Vomeronasal Organ of Pre-pubertal Pigs

Guiraudie-Capraz, G. (2003) · Chemical Senses · doi:10.1093/chemse/bjg052 · Cited by 56 · see citing works

Evolution of the lipocalin family as inferred from a protein sequence phylogeny

Gutiérrez, G., Ganfornina, M. D., & Sánchez, D. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00151-5 · Cited by 55 · see citing works

Apolipoprotein D levels are elevated in prefrontal cortex of subjects with Alzheimer’s disease

Thomas, E. A., Laws, S. M., Sutcliffe, J. G., Harper, C. G., Dean, B., McClean, C., Masters, C. L., Lautenschlager, N. T., Gandy, S., & Martins, R. N. (2003) · Biological Psychiatry · doi:10.1016/s0006-3223(02)01976-5 · Cited by 55 · see citing works

Studies on the quaternary structure of the lobster exoskeleton carotenoprotein, crustacyanin

Quarmby, R., Nordens, D. A., Zagalsky, P. F., Ceccaldi, H. J., & Daumas, R. A. (1977) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(77)90222-x · Cited by 54 · see citing works

Source and Cyclic Release Pattern of (Z)-7-Dodecenyl Acetate, the Pre-ovulatory Pheromone of the Female Asian Elephant

Rasmussen, L. E. L. (2001) · Chemical Senses · doi:10.1093/chemse/26.6.611 · Cited by 54 · see citing works

The de-epoxidase and epoxidase reactions of Mantoniella squamata (Prasinophyceae) exhibit different substrate-specific reaction kinetics compared to spinach

Frommolt, R., Goss, R., & Wilhelm, C. (2001) · Planta · doi:10.1007/s004250100589 · Cited by 53 · see citing works

Structural relationship of streptavidin to the calycin protein superfamily

Flower, D. R. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80382-5 · Cited by 53 · see citing works

Antisense Down-regulation of Lipocalin-interacting Membrane Receptor Expression Inhibits Cellular Internalization of Lipocalin-1 in Human NT2 Cells

Wojnar, P., Lechner, M., & Redl, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210922200 · Cited by 52 · see citing works

The crystal structure of the Escherichia coli lipocalin Blc suggests a possible role in phospholipid binding

Campanacci, V., Nurizzo, D., Spinelli, S., Valencia, C., Tegoni, M., & Cambillau, C. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00199-1 · Cited by 52 · see citing works

Violaxanthin accessibility and temperature dependency for de-epoxidation in spinach thylakoid membranes

Arvidsson, P., Carlsson, M., Stefánsson, H., Albertsson, P., & Åkerlund, H. (1997) · Photosynthesis Research · doi:10.1023/a:1005868026374 · Cited by 50 · see citing works

Intron distribution difference for 276 ancient and 131 modern genes suggests the existence of ancient introns

Fedorov, A. N., Cao, X., Saxonov, S., SOUZA, S. J. D., Roy, S. W., & Gilbert, W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.231491498 · Cited by 50 · see citing works

Chromosomal location, exon/intron organization and evolution of lipocalin genes

Salier, J. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00144-8 · Cited by 49 · see citing works

Substrate specificity of the violaxanthin de-epoxidase of the primitive green alga Mantoniella squamata (Prasinophyceae)

Goss, R. (2003) · Planta · doi:10.1007/s00425-003-1044-1 · Cited by 46 · see citing works

Lipocalin-type prostaglandin D synthase in milk: a new biomarker for bovine mastitis

Baeker, R., Haebel, S., Schlatterer, K., & Schlatterer, B. (2002) · Prostaglandins & Other Lipid Mediators · doi:10.1016/s0090-6980(01)00175-7 · Cited by 46 · see citing works

Binding of α1-Acid Glycoprotein to Membrane Results in a Unique Structural Change and Ligand Release

Nishi, K., Maruyama, T., Halsall, H. B., Handa, T., & Otagiri, M. (2004) · Biochemistry · doi:10.1021/bi0400204 · Cited by 45 · see citing works

Duocalins: Engineered Ligand-Binding Proteins with Dual Specificity Derived from the Lipocalin Fold

Schlehuber, S., & Skerra, A. (2001) · Biological Chemistry · doi:10.1515/bc.2001.166 · Cited by 43 · see citing works

Purification, cloning and characterisation of odorant- and pheromone-binding proteins from pig nasal epithelium

Scaloni, A., Paolini, S., Brandazza, A., Fantacci, M. E., Bottiglieri, C., Marchese, S., Navarrini, A., Fini, C., FERRARA, L., & Pelosi, P. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000903 · Cited by 42 · see citing works

LHCII, the major light-harvesting pigment-protein complex is a zeaxanthin epoxidase

Gruszecki, W. I., & Krupa, Z. (1993) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(93)90036-f · Cited by 42 · see citing works

Purification and properties of violaxanthin de-epoxidase from spinach

Havir, E. A., Tausta, S. L., & Peterson, R. B. (1997) · Plant Science · doi:10.1016/s0168-9452(97)04579-2 · Cited by 42 · see citing works

Site-directed mutagenesis of rat cellular retinol-binding protein

Stump, D. G., Lloyd, R. S., & Chytil, F. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64368-x · Cited by 42 · see citing works

Demonstration of a glycoprotein derived from the 24p3 gene in mouse uterine luminal fluid

Chu, S.-T., HUANG, H.-L., Jin-Mei, C. H. E. N., & Chen, Y. (1996) · Biochemical Journal · doi:10.1042/bj3160545 · Cited by 41 · see citing works

Presence of tear lipocalin and other major proteins in lacrimal fluid of rabbits

Azzarolo, A. M., Brew, K., Kota, S., Ponomareva, O. A., Schwartz, J., & Zylberberg, C. (2004) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpc.2004.02.012 · Cited by 39 · see citing works

A study of protein–carotenoid interactions in the astaxanthin-protein crustacyanin by absorption and Stark spectroscopy; evidence for the presence of three spectrally distinct species

Krawczyk, S., & Britton, G. (2001) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00242-9 · Cited by 39 · see citing works

Prostaglandin D2 synthase induces apoptosis in PC12 neuronal cells

Ragolia, L., Palaia, T. A., Frese, L., Fishbane, S., & Maesaka, J. K. (2001) · Neuroreport · doi:10.1097/00001756-200108280-00008 · Cited by 39 · see citing works

Enhancement of Lipocalin-Type Prostaglandin D Synthase Enzyme Activity by Guanidine Hydrochloride

Inui, T., Ohkubo, T., Urade, Y., & Hayaishi, O. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1881 · Cited by 38 · see citing works

Changes in salivary nitrophorin profile during the life cycle of the blood-sucking bug Rhodnius prolixus

Moreira, M. F., Coelho, H. S. L., Zingali, R. B., de Oliveira, P. L., & Masuda, H. (2002) · Insect Biochemistry and Molecular Biology · doi:10.1016/s0965-1748(02)00163-7 · Cited by 37 · see citing works

Predicting the kinetics of peptide-antibody interactions using a multivariate experimental design of sequence and chemical space

Andersson, K., Choulier, L., H�m�l�inen, M. D., Regenmortel, M. H. V. V., Altschuh, D., & Malmqvist, M. (2001) · Journal of Molecular Recognition · doi:10.1002/1099-1352(200101/02)14:1 · Cited by 37 · see citing works

Delivery of ferric ion to mouse spermatozoa is mediated by lipocalin internalization

Elangovan, N., Lee, Y., Tzeng, W.-F., & Chu, S.-T. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.05.091 · Cited by 36 · see citing works

Resolution of ligand positions by site‐directed tryptophan fluorescence in tear lipocalin

Gasymov, O. K., Abduragimov, A. R., Yusifov, T., & Glasgow, B. J. (2000) · Protein Science · doi:10.1110/ps.9.2.325 · Cited by 36 · see citing works

Unfolding of newly made retinol-binding protein by dithiothreitol. Sensitivity to retinoids.

Kaji, E. H., & Lodish, H. F. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80666-8 · Cited by 34 · see citing works

Hippocampal apolipoprotein D level depends on Braak stage and APOE genotype

Glöckner, F., & Ohm, T. G. (2003) · Neuroscience · doi:10.1016/s0306-4522(03)00529-3 · Cited by 33 · see citing works

Structural and drug-binding properties of α1-acid glycoprotein in reverse micelles

Nishi, K., Sakai, N., Komine, Y., Maruyama, T., Halsall, H. B., & Otagiri, M. (2002) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/s1570-9639(02)00465-x · Cited by 32 · see citing works

Proteases in cyst fluid from human gross cyst breast disease.

Kesner, L., YU, W., Bradlow, H. L., Breed, C. W., & Fleisher, M. (1988) · PubMed · Cited by 30 · see citing works

Nuclear envelope associated protein that binds telomeric DNAs

Podgornaya, O. I., Bugaeva, E. A., Voronin, A. P., Gilson, É., & Mitchell, A. (2000) · Molecular Reproduction and Development · doi:10.1002/1098-2795(200009)57:1 · Cited by 30 · see citing works

β-Trace protein in human cerebrospinal fluid: a diagnostic marker for N-glycosylation defects in brain

Grünewald, S., Huyben, K. M. L. C., de Jong, J. G. N., Smeitink, J. A. M., Rubio, E., Boers, G. H. J., Conradt, H. S., Wendel, U., & Wevers, R. A. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(99)00078-2 · Cited by 30 · see citing works

Unfolding and refolding of porcine odorant binding protein in guanidinium hydrochloride: equilibrium studies at neutral pH

Parisi, M., Mazzini, A., Sorbi, R. T., Ramoni, R., Grolli, S., & Favilla, R. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.08.009 · Cited by 30 · see citing works

Effect of monogalactosyldiacylglycerol and other thylakoid lipids on violaxanthin de-epoxidation in liposomes

Latowski, D., Kostecka, A., & Strzałka, K. (2000) · Biochemical Society Transactions · doi:10.1042/bst0280810 · Cited by 29 · see citing works

The interaction of N-ethyl retinamide with plasma retinol-binding protein (RBP) and the crystal structure of the retinoid-RBP complex at 1.9-A resolution.

Zanotti, G., Malpeli, G., & Berni, R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74546-3 · Cited by 28 · see citing works

THE INTERACTION OF N-ETHYL RETINAMIDE WITH PLASMA RETINOL-BINDING PROTEIN (RBP) AND THE CRYSTAL STRUCTURE OF THE RETINOID-RBP COMPLEX AT 1.9 ANGSTROMS RESOLUTION

Zanotti, G., & Berni, R. (1993) · Worldwide Protein Data Bank · doi:10.2210/pdb1erb/pdb · Cited by 27 · see citing works

Substrate Specificity and Functional Aspects of Violaxanthin-de-Epoxidase, an Enzyme of the Xanthophyll Cycle

Grotz, B., Molnár, P., Stransky, H., & Hager, A. (1999) · Journal of Plant Physiology · doi:10.1016/s0176-1617(99)80280-6 · Cited by 27 · see citing works

Human Lipocalin-1, a Physiological Scavenger of Lipophilic Compounds, Is Produced by Corticotrophs of the Pituitary Gland

Wojnar, P., Dirnhofer, S., Ladurner, P., Berger, P., & Redl, B. (2002) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215540205000314 · Cited by 27 · see citing works

Exon?intron structure of outlier tick lipocalins indicate a monophyletic origin within the larger lipocalin family

Mans, B. J., & Neitz, A. W. H. (2004) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2004.03.006 · Cited by 26 · see citing works

Prostaglandin D2 synthase induces apoptosis in pig kidney LLC-PK1 cells

Maesaka, J. K., Palaia, T. A., Frese, L., Fishbane, S., & Ragolia, L. (2001) · Kidney International · doi:10.1046/j.1523-1755.2001.00989.x · Cited by 25 · see citing works

Quaternary structure of alpha‐crustacyanin from lobster as seen by small‐angle X‐ray scattering

Dellisanti, C. D., Spinelli, S., Cambillau, C., Findlay, J. B. C., Zagalsky, P. F., Finet, S., & Receveur‐Brechot, V. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00486-1 · Cited by 25 · see citing works

Lazarillo, a neuronal lipocalin in grasshoppers with a role in axon guidance

Sánchez, D., Ganfornina, M. D., & Bastiani, M. J. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00146-1 · Cited by 23 · see citing works

Role of histidines in the binding of violaxanthin de‐epoxidase to the thylakoid membrane as studied by site‐directed mutagenesis

Gisselsson, A., Szilágyi, A., & Åkerlund, H. (2004) · Physiologia Plantarum · doi:10.1111/j.1399-3054.2004.00415.x · Cited by 23 · see citing works

Improved folding of apo-retinol-binding protein in the periplasm of Escherichia coli: positive influences of dsbC coexpression and of an amino acid exchange in the vitamin A binding site

Schmidt, A. M., Bloss, I., & Skerra, A. (1998) · Protein Engineering Design and Selection · doi:10.1093/protein/11.7.601 · Cited by 21 · see citing works

The transfer of transthyretin and receptor-binding properties from the plasma retinol-binding protein to the epididymal retinoic acid-binding protein

Sundaram, M., van Aalten, D. M. F., Findlay, J. B. C., & Sivaprasadarao, A. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3620265 · Cited by 20 · see citing works

Expression of Prostaglandin D Synthase in Ovarian Cancer

Su, B., Guan, M., Zhao, R., & Lu, Y. (2001) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2001.190 · Cited by 19 · see citing works

CALβ, a novel lipocalin associated with chondrogenesis and inflammation

Pagano, A., Giannoni, P., Zambotti, A., Randazzo, N., Zerega, B., Cancedda, R., & Dozin, B. (2002) · European Journal of Cell Biology · doi:10.1078/0171-9335-00243 · Cited by 18 · see citing works

Characterization of Violaxanthin De-Epoxidase Purified in the Presence of Tween 20: Effects of Dithiothreitol and Pepstatin A

Kuwabara, T., Hasegawa, M., Kawano, M., & Takaichi, S. (1999) · Plant and Cell Physiology · doi:10.1093/oxfordjournals.pcp.a029496 · Cited by 18 · see citing works

Dimerization, stability and electrostatic properties of porcine β‐lactoglobulin

Ugolini, R., Ragona, L., Silletti, E., Fogolari, F., Visschers, R. W., Alting, A. C., & Molinari, H. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02371.x · Cited by 17 · see citing works

A chondrogenesis-related lipocalin cluster includes a third new gene, CALγ

Pagano, A., Crooijmans, R. P. M. A., Groenen, M. A. M., Randazzo, N., Zerega, B., Cancedda, R., & Dozin, B. (2003) · Gene · doi:10.1016/s0378-1119(03)00382-2 · Cited by 16 · see citing works

Amphibian choroid plexus lipocalin, Cpl1

Lepperdinger, G. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00143-6 · Cited by 15 · see citing works

The lipocalin website

Paine, K., & Flower, D. R. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00166-7 · Cited by 14 · see citing works

Dicyclohexylcarbodiimide alters the pH dependence of violaxanthin de-epoxidation

Jahns, P., & Heyde, S. (1999) · Planta · doi:10.1007/s004250050497 · Cited by 14 · see citing works

Retinoids and Epididymal Function

Orgebin‐Crist, M., Lareyre, J., Suzuki, K., Araki, Y., Fouchécourt, S., Matusik, R. J., & Ong, D. E. (2002) · Springer eBooks · doi:10.1007/978-1-4615-0679-9_19 · Cited by 13 · see citing works

pH‐dependent reversible inhibition of violaxanthin de‐epoxidase by pepstatin related to protonation‐induced structural change of the enzyme

Kawano, M., & Kuwabara, T. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01991-8 · Cited by 12 · see citing works

Stimulation of lipocalin‐type prostaglandin D synthase by retinoic acid coincides with inhibition of cell proliferation in human 3AO ovarian cancer cells

Su, B., Guan, M., Xia, J., & Lu, Y. (2003) · Cell Biology International · doi:10.1016/s1065-6995(03)00100-8 · Cited by 12 · see citing works

Heterologous expression of bovine and porcine β-lactoglobulins in Pichia pastoris: towards a comparative functional characterisation

Invernizzi, G., Ragona, L., Brocca, S., Pedrazzoli, E., Molinari, H., Morandini, P. A., Catalano, M., & Lotti, M. (2004) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2003.10.034 · Cited by 12 · see citing works

Temperature-dependent osmotic permeability in glycoproteion containing liposomes

Neitchev, V. Z., & Bideaud, F. A. (1988) · Molecular Biology Reports · doi:10.1007/bf00539055 · Cited by 11 · see citing works

Changes in concanavalin A-reactive proteins in neurological disorders

Saso, L., Valentini, G., Leone, M. G., Grippa, E., Guglielmi, R., Paris, L., Cantore, G. P., & Silvestrini, B. (1999) · Journal of Clinical Laboratory Analysis · doi:10.1002/(sici)1098-2825(1999)13:4 · Cited by 11 · see citing works

Structure-function relationships of human apolipoprotein D An immunochemical analysis

Terrisse, L., Marcoux, K., Carmo, S. D., Brissette, L., Milne, R. W., & Rassart, É. (2001) · Life Sciences · doi:10.1016/s0024-3205(01)01439-4 · Cited by 10 · see citing works

Molecular crowding as a mechanism for tick secretory granule biogenesis

Mans, B. J., & Neitz, A. W. H. (2004) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2004.07.007 · Cited by 10 · see citing works

Phylogeny and regulation of four lipocalin genes clustered in the chicken genome: evidence of a functional diversification after gene duplication

Pagano, A., Giannoni, P., Zambotti, A., Sánchez, D., Ganfornina, M. D., Gutiérrez, G., Randazzo, N., Cancedda, R., & Dozin, B. (2004) · Gene · doi:10.1016/j.gene.2004.02.001 · Cited by 8 · see citing works

Analysis of the formation of the animal pole plasm in the eggs of Limnaea stagnalis

Raven, C. P., & Wal, U. P. V. D. (1964) · Development · doi:10.1242/dev.12.1.123 · Cited by 8 · see citing works

Gelling Properties of Heat-Denatured β-Lactoglobulin Aggregates in a High-Salt Buffer

Vittayanont, M., Steffe, J. F., Flegler, S. L., & Smith, D. M. (2002) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf011410p · Cited by 7 · see citing works

Lipocalin-type prostaglandin D synthase in cerebrospinal fluid of patients with aneurysmal subarachnoid hemorrhage scavenges bile pigments

Inui, T., Mase, M., Emi, M., Nakau, H., Seiki, K., Oda, H., Yamada, K., & Urade, Y. (2002) · International Congress Series · doi:10.1016/s0531-5131(02)00528-9 · Cited by 5 · see citing works

Crystal structure of lipocalin-type prostaglandin D synthase

Irikura, D., Kumasaka, T., Yamamoto, M., Hayaishi, O., & Urade, Y. (2002) · International Congress Series · doi:10.1016/s0531-5131(02)00527-7 · Cited by 2 · see citing works

Untitled work

(1999) · doi:10.1002/(sici)1098-1063(1999)9:2

Jasmonates: An Update on Biosynthesis, Signal Transduction and Action in Plant Stress Response, Growth and Development

Wasternack, C. H. (2007) · Annals of Botany · doi:10.1093/aob/mcm079 · Cited by 1,836 · see citing works

Biodiversity of NPQ

Goss, R., & Bernard, L. (2014) · Journal of Plant Physiology · doi:10.1016/j.jplph.2014.03.004 · Cited by 479 · see citing works

Regulation and function of xanthophyll cycle-dependent photoprotection in algae

Goss, R., & Jakob, T. (2010) · Photosynthesis Research · doi:10.1007/s11120-010-9536-x · Cited by 429 · see citing works

Mechanism and regulation of the violaxanthin cycle: The role of antenna proteins and membrane lipids

Jahns, P., Latowski, D., & Strzałka, K. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.09.013 · Cited by 402 · see citing works

Fatty acid transport proteins, implications in physiology and disease

Kazantzis, M., & Stahl, A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2011.09.010 · Cited by 276 · see citing works

Hepatokines and metabolism: Deciphering communication from the liver

Jensen-Cody, S. O., & Potthoff, M. J. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101138 · Cited by 252 · see citing works

Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?

Costa, J. S., Bavaro, S. L., Benedé, S., Díaz‐Perales, A., Bueno, C., Gelencsér, É., Klueber, J., Larré, C., Lozano‐Ojalvo, D., Lupi, R., et al. (2020) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-020-08810-9 · Cited by 181 · see citing works

Carotenoid biosynthesis in diatoms

Bertrand, M. (2010) · Photosynthesis Research · doi:10.1007/s11120-010-9589-x · Cited by 172 · see citing works

A Structural Basis for the pH-Dependent Xanthophyll Cycle in Arabidopsis thaliana

Arnoux, P., Morosinotto, T., Saga, G., Bassi, R., & Pignol, D. (2009) · The Plant Cell · doi:10.1105/tpc.109.068007 · Cited by 167 · see citing works

Apolipoprotein D takes center stage in the stress response of the aging and degenerative brain

Dassati, S., Waldner, A., & Schweigreiter, R. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.01.148 · Cited by 163 · see citing works

Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?

Costa, J. S., Villa, C., Verhoeckx, K. C. M., Veličković, T. Ć., Schrama, D., Roncada, P., Rodrigues, P. M., Piras, C., Martín‐Pedraza, L., Monaci, L., et al. (2021) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-020-08826-1 · Cited by 155 · see citing works

The Plastid Lipocalin LCNP Is Required for Sustained Photoprotective Energy Dissipation in Arabidopsis

Malnoë, A., Schultink, A., Shahrasbi, S., Rumeau, D., Havaux, M., & Niyogi, K. (2017) · The Plant Cell · doi:10.1105/tpc.17.00536 · Cited by 136 · see citing works

Transient Receptor Potential Channel Type M5 Is Essential for Fat Taste

Liu, P., Shah, B. P., Croasdell, S., & Gilbertson, T. A. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.6273-10.2011 · Cited by 125 · see citing works

Tear Lipocalin: structure and Function

Dartt, D. A. (2011) · The Ocular Surface · doi:10.1016/s1542-0124(11)70022-2 · Cited by 121 · see citing works

Eicosanoid Signaling in Insects: from Discovery to Plant Protection

STANLEY, D. W., & Kim, Y. (2014) · Critical Reviews in Plant Sciences · doi:10.1080/07352689.2014.847631 · Cited by 119 · see citing works

A1M, an extravascular tissue cleaning and housekeeping protein

Åkerström, B., & Gram, M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.06.025 · Cited by 96 · see citing works

The Crystal Structure of Arabidopsis thaliana Allene Oxide Cyclase: Insights into the Oxylipin Cyclization Reaction

Hofmann, E., Zerbe, P., & Schaller, F. (2006) · The Plant Cell · doi:10.1105/tpc.106.043984 · Cited by 96 · see citing works

Lipid Dependence of Xanthophyll Cycling in Higher Plants and Algae

Goss, R., & Latowski, D. (2020) · Frontiers in Plant Science · doi:10.3389/fpls.2020.00455 · Cited by 93 · see citing works

Neutrophil Gelatinase-Associated Lipocalin Is a Novel Mineralocorticoid Target in the Cardiovascular System

Latouche, C., Moghrabi, S. E., Messaoudi, S., Cat, A. N. D., Hernández-Díaz, I., de la Rosa, D. Á., Perret, C., López‐Andrés, N., Rossignol, P., Zannad, F. M., et al. (2012) · Hypertension · doi:10.1161/hypertensionaha.111.187872 · Cited by 91 · see citing works

Aldosterone Target NGAL (Neutrophil Gelatinase–Associated Lipocalin) Is Involved in Cardiac Remodeling After Myocardial Infarction Through NFκB Pathway

Martínez‐Martínez, E., Buonafine, M., Boukhalfa, I., Ibarrola, J., Fernández‐Celis, A., Kolkhof, P., Rossignol, P., Girerd, N., Mulder, P. G. H., López‐Andrés, N., et al. (2017) · Hypertension · doi:10.1161/hypertensionaha.117.09791 · Cited by 90 · see citing works

The chloroplastic lipocalin AtCHL prevents lipid peroxidation and protects Arabidopsis against oxidative stress

Levesque‐Tremblay, G., Havaux, M., & Ouellet, F. (2009) · The Plant Journal · doi:10.1111/j.1365-313x.2009.03991.x · Cited by 89 · see citing works

Animal Lipocalin Allergens

Hilger, C., Kuehn, A., & Hentges, F. (2012) · Current Allergy and Asthma Reports · doi:10.1007/s11882-012-0283-2 · Cited by 86 · see citing works

A rabidopsis lipocalins AtCHL and AtTIL have distinct but overlapping functions essential for lipid protection and seed longevity

Boca, S., KOESTLER, F., Ksas, B., Chevalier, A., Leymarie, J., Fekete, Á., Mueller, M. J., & Havaux, M. (2013) · Plant Cell & Environment · doi:10.1111/pce.12159 · Cited by 82 · see citing works

Role of MGDG and Non-bilayer Lipid Phases in the Structure and Dynamics of Chloroplast Thylakoid Membranes

Garab, G., Ughy, B., & Goss, R. (2016) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-25979-6_6 · Cited by 81 · see citing works

Local Reactions to Tick Bites

Castelli, E., Caputo, V., Morello, V., & Tomasino, R. M. (2008) · American Journal of Dermatopathology · doi:10.1097/dad.0b013e3181676b60 · Cited by 75 · see citing works

Phycobiliprotein Biosynthesis in Cyanobacteria: Structure and Function of Enzymes Involved in Post-translational Modification

Schluchter, W. M., Shen, G., Alvey, R. M., Biswas, A., Saunée, N. A., Williams, S. R., Mille, C. A., & Bryant, D. A. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-1528-3_12 · Cited by 74 · see citing works

The coat morphogenetic protein SpoVID is necessary for spore encasement in Bacillus subtilis

Wang, K. H., Isidro, A., Domingues, L., Eskandarian, H., McKenney, P. T., Drew, K., Grabowski, P. P., Chua, M.-H., Barry, S. N., Guan, M., et al. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06886.x · Cited by 80 · see citing works

Structural and functional roles of non-bilayer lipid phases of chloroplast thylakoid membranes and mitochondrial inner membranes

Garab, G., Yaguzhinsky, L. S., Dlouhý, O., Nesterov, S. V., Špunda, V., & Gasanoff, E. S. (2022) · Progress in Lipid Research · doi:10.1016/j.plipres.2022.101163 · Cited by 72 · see citing works

Elevated Serum Neutrophil Gelatinase-Associated Lipocalin Is an Early Predictor of Severity and Outcome in Acute Pancreatitis

Chakraborty, S., Kaur, S., Muddana, V. N., Sharma, N. R., Wittel, U. A., Papachristou, G. I., Whitcomb, D. C., Brand, R. E., & Batra, S. K. (2010) · The American Journal of Gastroenterology · doi:10.1038/ajg.2010.23 · Cited by 71 · see citing works

Allergens and their associated small molecule ligands—their dual role in sensitization

Chruszcz, M., Chew, F. T., Hoffmann‐Sommergruber, K., Hurlburt, B. K., Mueller, G. A., Pomés, A., Rouvinen, J., Villalba, M., Wöhrl, B. M., & Breiteneder, H. (2021) · Allergy · doi:10.1111/all.14861 · Cited by 70 · see citing works

An Integrated “Multi-Omics” Comparison of Embryo and Endosperm Tissue-Specific Features and Their Impact on Rice Seed Quality

Galland, M., He, D., Lounifi, I., Arc, E., Clément, G., Balzergue, S., Huguet, S., Cueff, G., Godin, B., Collet, B., et al. (2017) · Frontiers in Plant Science · doi:10.3389/fpls.2017.01984 · Cited by 70 · see citing works

Proteomic profiling of amniotic fluid in preterm labor using two-dimensional liquid separation and mass spectrometry

Bujold, E., Romero, R. J., Kusanovic, J. P., Erez, O., Gotsch, F., Chaiworapongsa, T., Gómez, R., Espinoza, J., Vaisbuch, E., Kim, Y. M., et al. (2008) · The Journal of Maternal-Fetal & Neonatal Medicine · doi:10.1080/14767050802053289 · Cited by 68 · see citing works

Plastid Proteomic Analysis in Tomato Fruit Development

Suzuki, M. M., Takahashi, S., Kondo, T., Dohra, H., Ito, Y., Kiriiwa, Y., Hayashi, M., Kamiya, S., Kato, M., Fujiwara, M., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0137266 · Cited by 66 · see citing works

Lipocalin family proteins and their diverse roles in cardiovascular disease

Yang, H., Wang, X., Li, S., Liu, Y., Akbar, R., & Fan, G. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108385 · Cited by 67 · see citing works

Respiratory Allergens from Furred Mammals: Environmental and Occupational Exposure

Zahradnik, E., & Raulf, M. (2017) · Veterinary Sciences · doi:10.3390/vetsci4030038 · Cited by 65 · see citing works

Temperature-induced lipocalin (TIL) is translocated under salt stress and protects chloroplasts from ion toxicity

Abo-Ogiala, A. M., Carsjens, C. S., Diekmann, H., Fayyaz, P., Herrfurth, C., Feußner, I., & Polle, A. (2013) · Journal of Plant Physiology · doi:10.1016/j.jplph.2013.08.003 · Cited by 61 · see citing works

Lipid polymorphism in chloroplast thylakoid membranes – as revealed by 31P-NMR and time-resolved merocyanine fluorescence spectroscopy

Garab, G., Ughy, B., de Waard, P., Akhtar, P., Javornik, U., Kotakis, C., Šket, P., Karlický, V., Materová, Z., Špunda, V., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-13574-y · Cited by 57 · see citing works

Activation of Several Key Components of the Epidermal Differentiation Pathway in Cattle Following Infestation with the Cattle Tick, Rhipicephalus (Boophilus) Microplus

Kongsuwan, K., Josh, P., Colgrave, M. L., Bagnall, N. H., Gough, J., Burns, B., & Pearson, R. (2010) · International Journal for Parasitology · doi:10.1016/j.ijpara.2009.10.013 · Cited by 48 · see citing works

Hydrophobic interactions and ionic networks play an important role in thermal stability and denaturation mechanism of the porcine odorant‐binding protein

Stepanenko, O. V., Marabotti, A., Kuznetsova, I. М., Константинович, Т. К., Fini, C., Varriale, A., Staiano, M., Rossi, M., & D’Auria, S. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21658 · Cited by 48 · see citing works

Stress-Induced Lipocalin-2 Controls Dendritic Spine Formation and Neuronal Activity in the Amygdala

Skrzypiec, A. E., Shah, R. S., Schiavon, E., Baker, E., Skene, N., Pawlak, R., & Mucha, M. W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061046 · Cited by 47 · see citing works

Molecular Characterisation of Colour Formation in the Prawn Fenneropenaeus merguiensis

Ertl, N. G., Elizur, A., Brooks, P. R., Kuballa, A., Anderson, T. A., & Knibb, W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056920 · Cited by 47 · see citing works

Age-related learning deficits can be reversible in honeybees Apis mellifera

Baker, N., Wolschin, F., & Amdam, G. V. (2012) · Experimental Gerontology · doi:10.1016/j.exger.2012.05.011 · Cited by 47 · see citing works

OsVDE, a xanthophyll cycle key enzyme, mediates abscisic acid biosynthesis and negatively regulates salinity tolerance in rice

Wang, X., Ren, P., Ji, L., Zhu, B., & Xie, G. (2021) · Planta · doi:10.1007/s00425-021-03802-1 · Cited by 47 · see citing works

Retinoid-Binding Proteins: Similar Protein Architectures Bind Similar Ligands via Completely Different Ways

Zhang, Y., Zhao, Y., & Huang, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036772 · Cited by 46 · see citing works

An atypical short-chain dehydrogenase–reductase functions in the relaxation of photoprotective qH in Arabidopsis

Amstutz, C. L., Fristedt, R., Schultink, A., Merchant, S., Niyogi, K., & Malnoë, A. (2020) · Nature Plants · doi:10.1038/s41477-020-0591-9 · Cited by 46 · see citing works

A model of dirigent proteins derived from structural and functional similarities with allene oxide cyclase and lipocalins

Pickel, B., Pfannstiel, J., Steudle, A., Lehmann, A., Gerken, U., Pleiss, J., & Schaller, A. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08580.x · Cited by 45 · see citing works

β-Lactoglobulin

Sawyer, L. (2012) · Springer eBooks · doi:10.1007/978-1-4614-4714-6_7 · Cited by 41 · see citing works

Structure-Based Phylogenetic Analysis of the Lipocalin Superfamily

Lakshmi, B. V., Mishra, M., Srinivasan, N., & Archunan, G. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135507 · Cited by 40 · see citing works

Role of Saliva in the Oral Processing of Food

Carpenter, G. H. (2012) · Wiley eBooks · doi:10.1002/9781444360943.ch3 · Cited by 37 · see citing works

Structure, Functions, and Implications of Selected Lipocalins in Human Disease

Chandrasekaran, P., Weiskirchen, S., & Weiskirchen, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25084290 · Cited by 38 · see citing works

Structural analysis ofBacillus pumilusphenolic acid decarboxylase, a lipocalin-fold enzyme

Matte, A., Große, S., Bergeron, H., Abokitse, K., & Lau, P. C. K. (2010) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s174430911003246x · Cited by 35 · see citing works

Molecular mechanism of enzymatic allene oxide cyclization in plants

Hofmann, E., & Pollmann, S. (2008) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2007.12.007 · Cited by 35 · see citing works

Sphingolipid transfer proteins defined by the GLTP-fold

Malinina, L. V., Simanshu, D. K., Zhai, X., Самыгина, В. Р., Kamlekar, R. K., Kenoth, R., Ochoa-Lizarralde, B., Malakhova, M. L., Molotkovsky, J. G., Patel, D. J., et al. (2015) · Quarterly Reviews of Biophysics · doi:10.1017/s003358351400016x · Cited by 35 · see citing works

The OsTIL1 lipocalin protects cell membranes from reactive oxygen species damage and maintains the 18:3‐containing glycerolipid biosynthesis under cold stress in rice

Ji, L., Zhang, Z., Liu, S., Liyan, Z., Li, Q., Xiao, B., Suzuki, N., Burks, D. J., Azad, R. K., & Xie, G. (2023) · The Plant Journal · doi:10.1111/tpj.16470 · Cited by 33 · see citing works

Structural and Biochemical Characterization of the Bilin Lyase CpcS from Thermosynechococcus elongatus

Kronfel, C. M., Kuzin, A. P., Forouhar, F., Biswas, A., Su, M., Lew, S., Seetharaman, J., Xiao, R., Everett, J. K., Ma, L.-C., et al. (2013) · Biochemistry · doi:10.1021/bi401192z · Cited by 33 · see citing works

Recent advances in the development of novel protein scaffolds based therapeutics

Azhar, A., Ahmad, E., Zia, Q., Rauf, M. A., Owais, M., & Ashraf, G. M. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.04.045 · Cited by 33 · see citing works

Laurdan fluorescence spectroscopy in the thylakoid bilayer: The effect of violaxanthin to zeaxanthin conversion on the galactolipid dominated lipid environment

Szilágyi, A., Selstam, E., & Åkerlund, H. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.10.006 · Cited by 33 · see citing works

A systematic analysis of human lipocalin family and its expression in esophageal carcinoma

Du, Z., Wu, B., Wu, X., Lin, X., Qiu, X., Zhan, X.-F., Wang, S., Shen, J., Zheng, C.-P., Wu, Z., et al. (2015) · Scientific Reports · doi:10.1038/srep12010 · Cited by 34 · see citing works

Enthalpy/Entropy Compensation Effects from Cavity Desolvation Underpin Broad Ligand Binding Selectivity for Rat Odorant Binding Protein 3

Portman, K. L., Long, J., Carr, S. B., Briand, L. V., Winzor, D. J., Searle, M. S., & Scott, D. J. (2014) · Biochemistry · doi:10.1021/bi5002344 · Cited by 32 · see citing works

Gustatory Mechanisms for Fat Detection

Gilbertson, T. A., Yu, T., & Shah, B. P. (2009) · Frontiers in neuroscience · doi:10.1201/9781420067767-c3 · Cited by 32 · see citing works

Intestinal Saturated Long-Chain Fatty Acid, Glucose and Fructose Transporters and Their Inhibition by Natural Plant Extracts in Caco-2 Cells

Schreck, K., & Melzig, M. F. (2018) · Molecules · doi:10.3390/molecules23102544 · Cited by 32 · see citing works

Expression and function analysis of crustacyanin gene family involved in resistance to heavy metal stress and body color formation in Exopalaemon carinicauda

Gao, H., Ma, H., Sun, J., Xu, W., Gao, W., Lai, X., & Yan, B. (2021) · Journal of Experimental Zoology Part B Molecular and Developmental Evolution · doi:10.1002/jez.b.23025 · Cited by 32 · see citing works

Laser-captured microdissection-microarray analysis of the genes involved in endometrial carcinogenesis: stepwise up-regulation of lipocalin2 expression in normal and neoplastic endometria and its functional relevance

Miyamoto, T., Kashima, H., 鈴木, 昭., Kikuchi, N., Konishi, I., Seki, N., & Shiozawa, T. (2011) · Human Pathology · doi:10.1016/j.humpath.2010.07.027 · Cited by 32 · see citing works

The Role of α1-Microglobulin (A1M) in Erythropoiesis and Erythrocyte Homeostasis—Therapeutic Opportunities in Hemolytic Conditions

Kristiansson, A., Gram, M., Flygare, J., Hansson, S. R., Åkerström, B., & Storry, J. R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197234 · Cited by 31 · see citing works

Evaluation of two new recombinant guinea‐pig lipocalins, Cav p 2 and Cav p 3, in the diagnosis of guinea‐pig allergy

Hilger, C., Swiontek, K., Kler, S., Diederich, C., Lehners, C., Vogel, L., Vieths, S., & Hentges, F. (2011) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2011.03726.x · Cited by 30 · see citing works

A developmentally regulated lipocalin-like gene is overexpressed in Tomato yellow leaf curl virus-resistant tomato plants upon virus inoculation, and its silencing abolishes resistance

Sade, D., Eybishtz, A., Gorovits, R., Sobol, I., & Czosnek, H. H. (2012) · Plant Molecular Biology · doi:10.1007/s11103-012-9946-6 · Cited by 30 · see citing works

Lipocalin 13 regulation of glucose and lipid metabolism in obesity

Zhou, Y., & Rui, L. (2013) · Vitamins & Hormones · doi:10.1016/b978-0-12-407766-9.00015-8 · Cited by 28 · see citing works

Phycobiliproteins in Microalgae: Occurrence, Distribution, and Biosynthesis

Kannaujiya, V. K., Singh, P. R., Kumar, D., & Sinha, R. P. (2020) · Pigments from Microalgae Handbook · doi:10.1007/978-3-030-50971-2_3 · Cited by 28 · see citing works

Differences in binding behavior of (−)-epigallocatechin gallate to β-lactoglobulin heterodimers (AB) compared to homodimers (A) and (B)

Keppler, J. K., Martin, D., Garamus, V. M., & Schwarz, K. (2015) · Journal of Molecular Recognition · doi:10.1002/jmr.2480 · Cited by 28 · see citing works

A hydrophobic proline-rich motif is involved in the intracellular targeting of temperature-induced lipocalin

Hernández-Gras, F., & Boronat, A. (2015) · Plant Molecular Biology · doi:10.1007/s11103-015-0326-x · Cited by 27 · see citing works

The fluid-mosaic membrane theory in the context of photosynthetic membranes: Is the thylakoid membrane more like a mixed crystal or like a fluid?

Wilhelm, C., Goss, R., & Garab, G. (2020) · Journal of Plant Physiology · doi:10.1016/j.jplph.2020.153246 · Cited by 27 · see citing works

Identification of new altered genes in rat cochleae with noise-induced hearing loss

Han, Y., Hong, L., Zhong, C., Chen, Y., Wang, Y., Mao, X., Zhao, D., & Qiu, J. (2012) · Gene · doi:10.1016/j.gene.2012.02.042 · Cited by 27 · see citing works

β-Lactoglobulin associative interactions: a small-angle scattering study

Anghel, L., Rogachev, A. V., Kuklin, A. I., & Erhan, R. V. (2019) · European Biophysics Journal · doi:10.1007/s00249-019-01360-9 · Cited by 26 · see citing works

Evidence that immunization with TP0751, a bipartite Treponema pallidum lipoprotein with an intrinsically disordered region and lipocalin fold, fails to protect in the rabbit model of experimental syphilis

Luthra, A., Montezuma-Rusca, J. M., Vake, C. J. L., LeDoyt, M., Delgado, K. N., Davenport, T. C., Fiel-Gan, M. D., Caimano, M. J., Radolf, J. D., & Hawley, K. L. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008871 · Cited by 25 · see citing works

Quantitative Proteomics Analysis ofCamelina sativaSeeds Overexpressing theAGG3Gene to Identify the Proteomic Basis of Increased Yield and Stress Tolerance

Alvarez, S., Choudhury, S. R., Sivagnanam, K., Hicks, L. M., & Pandey, S. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00150 · Cited by 26 · see citing works

Proteomic profiling in Lipocalin 2 deficient mice under normal and inflammatory conditions

Labbus, K., Henning, M., Borkham‐Kamphorst, E., Geisler, C., Berger, T., Mak, T. W., Knüchel, R., Meyer, H. E., Weiskirchen, R., & Henkel, C. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.11.021 · Cited by 25 · see citing works

Neutrophil gelatinase‐associated lipocalin: An early biomarker for predicting acute kidney injury and severity in patients with acute pancreatitis

Siddappa, P. K., Kochhar, R. K., Sarotra, P., Medhi, B., Jha, V., & Gupta, V. (2018) · JGH Open · doi:10.1002/jgh3.12112 · Cited by 26 · see citing works

Prawn lipocalin: characterization of a color shift induced by gene knockdown and ligand binding assay

Yang, F., Wang, M., Ma, Y., Ma, W., & Yang, W. (2011) · Journal of Experimental Zoology Part A Ecological Genetics and Physiology · doi:10.1002/jez.706 · Cited by 25 · see citing works

Comparison of α-Helix and β-Sheet Structure Adaptation to a Quantum Dot Geometry: Toward the Identification of an Optimal Motif for a Protein Nanoparticle Cover

Kopeć, K., Pędziwiatr, M., Gront, D., Sztatelman, O., Sławski, J., Łazicka, M., Worch, R., Zawada, K. D., Makarova, K., Nyk, M., et al. (2019) · ACS Omega · doi:10.1021/acsomega.9b00505 · Cited by 24 · see citing works

Structure of the Archaeal Pab87 Peptidase Reveals a Novel Self-Compartmentalizing Protease Family

Delfosse, V., Girard, É., Birck, C., Delmarcelle, M., Delarue, M. H., Poch, O., Schultz, P., & Mayer, C. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004712 · Cited by 24 · see citing works

High resolution X‐ray structures of mouse major urinary protein nasal isoform in complex with pheromones

Perez‐Miller, S., Zou, Q., Novotný, M. V., & Hurley, T. D. (2010) · Protein Science · doi:10.1002/pro.426 · Cited by 24 · see citing works

Impaired sperm maturation in conditional Lcn6 knockout mice†

Yin, Q., Shen, J., Wan, X., Liu, Q., Zhou, Y., & Zhang, Y. (2017) · Biology of Reproduction · doi:10.1093/biolre/iox128 · Cited by 24 · see citing works

Module structure of interphotoreceptor retinoid-binding protein (IRBP) may provide bases for its complex role in the visual cycle – structure/function study of Xenopus IRBP

Gonzalez-Fernandez, F., Baer, C. A., & Ghosh, D. (2007) · BMC Biochemistry · doi:10.1186/1471-2091-8-15 · Cited by 23 · see citing works

Identification and characterization of the lipid-binding property of GrlR, a locus of enterocyte effacement regulator

Jobichen, C., Fernandis, A. Z., Velázquez‐Campoy, A., Leung, K. Y., Mok, Y., Wenk, M. R., & Sivaraman, J. (2009) · Biochemical Journal · doi:10.1042/bj20081588 · Cited by 23 · see citing works

Membrane curvature stress controls the maximal conversion of violaxanthin to zeaxanthin in the violaxanthin cycle—influence of α-tocopherol, cetylethers, linolenic acid, and temperature

Szilágyi, A., Sommarin, M., & Åkerlund, H. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.06.001 · Cited by 23 · see citing works

Addition of β-Lactoglobulin Produces Water-Soluble Shikonin

Albreht, A., Vovk, I., & Simonovska, B. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf303153d · Cited by 22 · see citing works

How α-Helical Motifs Form Functionally Diverse Lipid-Binding Compartments

Malinina, L. V., Patel, D. J., & Brown, R. E. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044445 · Cited by 21 · see citing works

HDX‐MS reveals orthosteric and allosteric changes in apolipoprotein‐D structural dynamics upon binding of progesterone

Kielkopf, C. S., Ghosh, M., Anand, G. S., & Brown, S. H. J. (2018) · Protein Science · doi:10.1002/pro.3534 · Cited by 20 · see citing works

Discovery and Structural Analysis to Improve the Enantioselectivity of Hydroxynitrile Lyase from Parafontaria laminata Millipedes for ( R )-2-Chloromandelonitrile Synthesis

Nuylert, A., Nakabayashi, M., Yamaguchi, T., & Asano, Y. (2020) · ACS Omega · doi:10.1021/acsomega.0c03070 · Cited by 20 · see citing works

Structure of the first representative of Pfam family PF09410 (DUF2006) reveals a structural signature of the calycin superfamily that suggests a role in lipid metabolism

Chiu, H., Bakolitsa, C., Skerra, A., Lomize, A. L., Carlton, D. D., Miller, M. D., Krishna, S., Abdubek, P., Astakhova, T., Axelrod, H. L., et al. (2009) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309109037749 · Cited by 20 · see citing works

Male-specific protein (MSP): A new gene linked to sexual behavior and aggressiveness of tilapia males

Machnes, Z. M., Avtalion, R. R., Shirak, A., Trombka, D., Wides, R., Fellous, M., & Don, J. (2008) · Hormones and Behavior · doi:10.1016/j.yhbeh.2008.03.014 · Cited by 19 · see citing works

Applicability of analytical and preparative monolithic columns to the separation and isolation of major whey proteins

Albreht, A., & Vovk, I. (2012) · Journal of Chromatography A · doi:10.1016/j.chroma.2012.01.011 · Cited by 19 · see citing works

Membrane Barrels Are Taller, Fatter, Inside-Out Soluble Barrels

Dhar, R., Feehan, R., & Slusky, J. S. G. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c00878 · Cited by 18 · see citing works

The Factor H Binding Protein of Neisseria meningitidis Interacts with Xenosiderophores in Vitro

Veggi, D., Gentile, M. A., Cantini, F., Surdo, P. L., Nardi‐Dei, V., Seib, K. L., Pizza, M., Rappuoli, R., Banci, L., Savino, S., et al. (2012) · Biochemistry · doi:10.1021/bi301161w · Cited by 18 · see citing works

Structural and dynamic roles of permanent water molecules in ligand molecular recognition by chicken liver bile acid binding protein

Ricchiuto, P., Rocco, A. G., Gianazza, E., Corrada, D., Beringhelli, T., & Eberini, I. (2008) · Journal of Molecular Recognition · doi:10.1002/jmr.908 · Cited by 18 · see citing works

Exploring the molecular complexity of Triatoma dimidiata sialome

Santiago, P. B., de Araújo, C. N., Charneau, S. O., Bastos, I. M. D., Assumpção, T. C. F., Queiroz, R. M. L., Praça, Y. R., Cordeiro, T. D. M., Saraiva-Garcia, C., da Silva, I. G., et al. (2017) · Journal of Proteomics · doi:10.1016/j.jprot.2017.12.016 · Cited by 18 · see citing works

Wild-Type and Mutant Bovine Odorant-Binding Proteins To Probe the Role of the Quaternary Structure Organization in the Protein Thermal Stability

Marabotti, A., Scirè, A., Staiano, M., Crescenzo, R., Aurilia, V., Tanfani, F., & D’Auria, S. (2008) · Journal of Proteome Research · doi:10.1021/pr800528b · Cited by 18 · see citing works

Immunomodulatory Proteins in Tick Saliva From a Structural Perspective

Denisov, S. S., & Dijkgraaf, I. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.769574 · Cited by 19 · see citing works

R ‐hydroxynitrile lyase from the cyanogenic millipede, Chamberlinius hualienensis —A new entry to the carrier protein family Lipocalines

Motojima, F., Izumi, A., Nuylert, A., Zhai, Z., Dadashipour, M., Shichida, S., Yamaguchi, T., Nakano, S., & Asano, Y. (2020) · FEBS Journal · doi:10.1111/febs.15490 · Cited by 17 · see citing works

The lipocalin protein family: structure and function

FLOWER, D. R. (1996) · Biochemical Journal · doi:10.1042/bj3180001 · Cited by 1,679 · see citing works

Bacterial Lipocalins: Origin, Structure, and Function

Akerstrom, B. (2006) · CRC Press eBooks · doi:10.1201/9781498712736-9 · Cited by 8 · see citing works

The Menagerie of Human Lipocalins: A Natural Protein Scaffold for Molecular Recognition of Physiological Compounds

Schiefner, A., & Skerra, A. (2015) · Accounts of Chemical Research · doi:10.1021/ar5003973 · Cited by 97 · see citing works

Lipocalin

Thévenod, F. (2014) · Springer eBooks · doi:10.1007/978-3-642-27841-9_7077-4

Structure, function and medical significance of lipocalins

Fořtová, M., Průša, R., & Vajtr, D. (2013) · Klinická biochemie a metabolismus · doi:10.61568/kbm.2013.022