The lipocalin protein family: structure and function

FLOWER, Darren R.

doi:10.1042/bj3180001

Cited by 1,679Protein Interaction Studies and Fluorescence AnalysisProtein Structure and DynamicsEnzyme Structure and Function

The lipocalin protein family: structure and function

Open access

FLOWER, Darren R.·1996·Biochemical Journal

DOI 10.1042/bj3180001PMC PMC1217580

Open this paper in CoChat — free account Open PDF

Abstract

The lipocalin protein family is a large group of small extracellular proteins. The family demonstrates great diversity at the sequence level; however, most lipocalins share three characteristic conserved sequence motifs, the kernel lipocalins, while a group of more divergent family members, the outlier lipocalins, share only one. Belying this sequence dissimilarity, lipocalin crystal structures are highly conserved and comprise a single eight-stranded continuously hydrogen-bonded antiparallel beta-barrel, which encloses an internal ligand-binding site. Together with two other families of ligand-binding proteins, the fatty-acid-binding proteins (FABPs) and the avidins, the lipocalins form part of an overall structural superfamily: the calycins. Members of the lipocalin family are characterized by several common molecular-recognition properties: the ability to bind a range of small hydrophobic molecules, binding to specific cell-surface receptors and the formation of complexes with soluble macromolecules. The varied biological functions of the lipocalins are mediated by one or more of these properties. In the past, the lipocalins have been classified as transport proteins; however, it is now clear that the lipocalins exhibit great functional diversity, with roles in retinol transport, invertebrate cryptic coloration, olfaction and pheromone transport, and prostaglandin synthesis. The lipocalins have also been implicated in the regulation of cell homoeostasis and the modulation of the immune response, and, as carrier proteins, to act in the general clearance of endogenous and exogenous compounds.

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

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

Integrity signals

Registry

Crossref · 10.1042/bj3180001

Cites

142 of 142 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

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

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

Claims other papers make about this one

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

LCN proteins are secreted proteins that bind small hydrophobic ligands through their conical β barrels.
“Lipocalin (LCN) proteins are secreted proteins that bind small hydrophobic ligands through their conical β barrels [252,253].”
From Hepatokines and metabolism: Deciphering communication from the liver (2021) · cites this paper as [253]

Self-check

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

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

Comprehensive insect physiology, biochemistry and pharmacology
Brooks, G. T. (1985) · Insect Biochemistry · doi:10.1016/0020-1790(85)90131-3 · Cited by 1,597 · see citing works
Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase
Kjeldsen, L., Johnsen, A., Sengeløv, H., & Borregaard, N. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82217-7 · Cited by 1,286 · see citing works
The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein
Papiz, M. Z., Sawyer, L., Eliopoulos, E., North, A. C. T., Findlay, J. B. C., Sivaprasadarao, A., Jones, T. A., Newcomer, M. E., & Kraulis, P. J. (1986) · Nature · doi:10.1038/324383a0 · Cited by 873 · see citing works
Transport and Storage of Vitamin A
Blomhoff, R., Green, M. H., Berg, T., & Norum, K. R. (1990) · Science · doi:10.1126/science.2218545 · Cited by 609 · see citing works
Drug binding to human alpha-1-acid glycoprotein in health and disease.
Kremer, J. M., Wilting, J., & Janssen, L. H. M. (1988) · Pharmacological Reviews · doi:10.1016/s0031-6997(25)00015-8 · Cited by 584 · see citing works
Advanced Dairy Chemistry
McSweeney, P. L. H., & Fox, P. F. (2013) · Springer eBooks · doi:10.1007/978-1-4614-4714-6 · Cited by 502 · see citing works
Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein
Monaco, H. L., Rizzi, M., & Coda, A. (1995) · Science · doi:10.1126/science.7754382 · Cited by 410 · see citing works
Binding Affinities of Retinol and Related Compounds to Retinol Binding Proteins
Cogan, U., Kopelman, M., Mokady, S., & Shinitzky, M. (1976) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1976.tb10390.x · Cited by 381 · see citing works
Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography
Böcskei, Z., Groom, C. R., Flower, D. R., Wright, C. E., Phillips, S. E. V., Cavaggioni, A., Findlay, J. B. C., & North, A. C. T. (1992) · Nature · doi:10.1038/360186a0 · Cited by 361 · 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
Retinol-Binding Protein: The Serum Transport Protein for Vitamin A*
Blaner, W. S. (1989) · Endocrine Reviews · doi:10.1210/edrv-10-3-308 · Cited by 316 · see citing works
Crystallographic refinement of human serum retinol binding protein at 2Å resolution
Cowan, S. W., Newcomer, M. E., & Jones, T. A. (1990) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340080108 · Cited by 310 · see citing works
Distribution and Functions of Lecithin: Cholesterol Acyltransferase and Cholesteryl Ester Transfer Protein in Plasma Lipoproteins
Francone, O. L., Gürakar, A. R., & Fielding, C. J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83541-4 · Cited by 280 · see citing works
Homology of β-Lactoglobulin, Serum Retinol-Binding Protein, and Protein HC
Pervaiz, S., & Brew, K. (1985) · Science · doi:10.1126/science.2580349 · Cited by 260 · see citing works
Accumulation of apolipoproteins in the regenerating and remyelinating mammalian peripheral nerve. Identification of apolipoprotein D, apolipoprotein A-IV, apolipoprotein E, and apolipoprotein A-I.
Boyles, J. K., Notterpek, L. M., & Anderson, L. J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)38235-8 · Cited by 250 · see citing works
Identification of a New Acute Phase Protein
Liu, Q., & Nilsen‐Hamilton, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.38.22565 · Cited by 249 · see citing works
Molecular Cloning of Odorant-Binding Protein: Member of a Ligand Carrier Family
Pevsner, J., Reed, R. R., Feinstein, P. G., & Snyder, S. H. (1988) · Science · doi:10.1126/science.3388043 · Cited by 247 · see citing works
Suppression by human placental protein 14 of natural killer cell activity
OKAMOTO, N., UCHIDA, A., TAKAKURA, K., KARIYA, Y., KANZAKI, H., RIITTINEN, L., KOISTINEN, R., SEPPÄLÄ, M., & MORI, T. (1991) · American Journal of Reproductive Immunology · doi:10.1111/j.1600-0897.1991.tb00713.x · Cited by 234 · 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
Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 Å resolution
Huber, R., Schneider, M., Mayr, I., Müller, R., Deutzmann, R., Suter, F., Zuber, H., Falk, H., & Kayser, H. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90296-8 · Cited by 224 · see citing works
Inflammation-induced expression of sialyl Lewis X-containing glycan structures on alpha 1-acid glycoprotein (orosomucoid) in human sera.
de Graaf, T. W., van der Stelt, M. E., Anbergen, M. G., & van Dijk, W. (1993) · The Journal of Experimental Medicine · doi:10.1084/jem.177.3.657 · Cited by 224 · see citing works
Pheromone binding proteins of the mouse,Mus musculus
Bacchini, A., Gaetani, E., & Cavaggioni, A. (1992) · Cellular and Molecular Life Sciences · doi:10.1007/bf01923448 · Cited by 223 · see citing works
Identification of placental protein 14 as an immunosuppressive factor in human reproduction
Bolton, A. E., Clough, K. J., Stoker, R. J., Pockley, A. G., Mowles, E. A., Westwood, O. M. R., & Chapman, M. G. (1987) · The Lancet · doi:10.1016/s0140-6736(87)90235-2 · Cited by 220 · see citing works
The lipocalin protein family: A role in cell regulation
Flower, D. R. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01078-1 · Cited by 204 · see citing works
The molecular structure of insecticyanin from the tobacco hornworm Manduca sexta L. at 2.6 A resolution.
Holden, H. M., Rypniewski, W. R., Law, J. H., & Rayment, I. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02401.x · Cited by 197 · see citing works
Immunosuppression by human plasma alpha 1-acid glycoprotein: importance of the carbohydrate moiety.
Bennett, M., & Schmid, K. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.10.6109 · Cited by 186 · see citing works
The gene family for major urinary proteins: Expression in several secretory tissues of the mouse
Shaw, P. H., Held, W. A., & Hastie, N. D. (1983) · Cell · doi:10.1016/0092-8674(83)90061-2 · Cited by 180 · see citing works
Acceleration of puberty onset in female mice by male urinary proteins.
Mucignat‐Caretta, C., Caretta, A., & Cavaggioni, A. (1995) · The Journal of Physiology · doi:10.1113/jphysiol.1995.sp020830 · Cited by 180 · see citing works
Human brain prostaglandin D synthase has been evolutionarily differentiated from lipophilic-ligand carrier proteins.
Nagata, A., Suzuki, Y., Igarashi, M., Eguchi, N., Toh, H., Urade, Y., & Hayaishi, O. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.9.4020 · Cited by 175 · see citing works
Isolation and characterization of an olfactory receptor protein for odorant pyrazines.
Pevsner, J., Trifiletti, R. R., Strittmatter, S. M., & Snyder, S. H. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.9.3050 · Cited by 175 · see citing works
Tear lipocalins bind a broad array of lipid ligands
Glasgow, B. J., Abduragimov, A. R., Farahbakhsh, Z. T., Faull, K. F., & Hubbell, W. L. (1995) · Current Eye Research · doi:10.3109/02713689508999934 · Cited by 171 · see citing works
Biochemical Mechanisms and Pathobiology of α2u-Globulin Nephropathy
Borghoff, S. J., Short, B. G., & Swenberg, J. A. (1990) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.30.040190.002025 · Cited by 170 · see citing works
Carotenoid Chemistry and Biochemistry
(1982) · Elsevier eBooks · doi:10.1016/c2013-0-10173-0 · Cited by 166 · see citing works
Possible role for salivary gland protein in taste reception indicated by homology to lipophilic-ligand carrier proteins
Schmale, H., Holtgreve-Grez, H., & Christiansen, H. (1990) · Nature · doi:10.1038/343366a0 · Cited by 162 · see citing works
Crystallization, crystal structure analysis and preliminary molecular model of the bilin binding protein from the insect Pieris brassicae
Huber, R., Schneider, M., Epp, O., Mayr, I., Messerschmidt, A., Pflugrath, J. W., & Kayser, H. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90661-9 · Cited by 160 · see citing works
SV40-induced expression of mouse gene 24p3 involves a post-transcriptional mechanism.
Hraba-Renevey, S., Türler, H., Kress, M., Salomon, C., & Weil, R. (1989) · PubMed · Cited by 151 · see citing works
Complete amino acid sequence of human placental protein 14: a progesterone-regulated uterine protein homologous to beta-lactoglobulins.
Julkunen, M., Seppälä, M. T., & Jänne, O. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.23.8845 · Cited by 145 · see citing works
cDNA cloning and sequencing reveals human tear prealbumin to be a member of the lipophilic-ligand carrier protein superfamily.
Redl, B., Holzfeind, P. J., & Lottspeich, F. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)88698-2 · Cited by 142 · see citing works
Proof of the hepatic synthesis of a sex-dependent protein in the rat☆
Roy, A. K., & Neuhaus, O. W. (1966) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(66)90478-8 · Cited by 137 · see citing works
Arachidonic acid binds to apolipoprotein D: implications for the protein's function
Morais-Cabral, J. H., Atkins, G. L., Sánchez, L. M., López-Boado, Y. S., López-Otı́n, C., & Sawyer, L. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00484-q · Cited by 135 · see citing works
An intriguing member of the lipocalin protein family: α1-microglobulin
Åkerström, B., & Lögdberg, L. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90037-c · Cited by 135 · see citing works
Inhibition of platelet aggregation by native and desialised alpha-1 acid glycoprotein
Costello, M. J., Fiedel, B. A., & Gewurz, H. (1979) · Nature · doi:10.1038/281677a0 · Cited by 133 · see citing works
Identification by microsequencing of lipopolysaccharide-induced proteins secreted by mouse macrophages.
Meheus, L., Fransen, L. M., Raymackers, J., Blockx, H., BEEUMEN, J. V., Bun, S. M. V., & VOORDE, A. V. D. (1993) · The Journal of Immunology · doi:10.4049/jimmunol.151.3.1535 · Cited by 131 · see citing works
Cloning of Cockroach Allergen, Bla g 4, Identifies Ligand Binding Proteins (or Calycins) as a Cause of IgE Antibody Responses
Arruda, L. K., Vailes, L. D., Hayden, M. L., Benjamin, D. C., & Chapman, M. D. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.52.31196 · Cited by 131 · see citing works
Characterization of a plasma retinol-binding protein membrane receptor expressed in the retinal pigment epithelium
Båvik, C., Busch, C., & Eriksson, U. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50052-1 · Cited by 129 · see citing works
A complex-forming glycoprotein heterogeneous in charge and present in human plasma, urine, and cerebrospinal fluid
Tejler, L., & GRUBB, A. O. (1976) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(76)90164-1 · Cited by 129 · see citing works
Interactions of retinol with binding proteins: implications for the mechanism of uptake by cells
Noy, N., & Xu, Z. (1990) · Biochemistry · doi:10.1021/bi00468a012 · Cited by 127 · see citing works
Purification and analysis of a proteinaceous aphrodisiac pheromone from hamster vaginal discharge.
Singer, A. G., Macrides, F., Clancy, A. N., & Agosta, W. C. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69307-x · Cited by 125 · see citing works
Isolation of an Olfactory cDNA: Similarity to Retinol-Binding Protein Suggests a Role in Olfaction
Lee, K.-H., Wells, R. G., & Reed, R. R. (1987) · Science · doi:10.1126/science.3493528 · Cited by 124 · see citing works
Interactions of retinol with binding proteins: studies with rat cellular retinol-binding protein and with rat retinol-binding protein
Noy, N., & Blaner, W. S. (1991) · Biochemistry · doi:10.1021/bi00240a005 · Cited by 123 · see citing works
Differential, Multihormonal Regulation of the Mouse Major Urinary Protein Gene Family in the Liver
Knopf, J. L., Gallagher, J. F., & Held, W. A. (1983) · Molecular and Cellular Biology · doi:10.1128/mcb.3.12.2232-2240.1983 · Cited by 120 · see citing works
Regeneration‐associated high level expression of apolipoprotein D mRNA in endoneurial fibroblasts of peripheral nerve.
Spreyer, P., Schaal, H., Kuhn, H. G., Rothe, T., Unterbeck, A., Olek, K., & Müller, H. W. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07426.x · 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
Mouse oncogene protein 24p3 is a member of the Lipocalin protein family
Flower, D. R., North, A. C. T., & Attwood, T. K. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)81256-2 · Cited by 114 · 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
β‐Lactoglobulin binds retinol and protoporphyrin IX at two different binding sites
Dufour, É., Marden, M. C., & Haertlé, T. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80850-i · Cited by 110 · see citing works
The covalent protein structure of insecticyanin, a blue biliprotein from the hemolymph of the tobacco hornworm, Manduca sexta L.
Riley, C. T., Barbeau, B. K., Keim, P. S., Kezdy, F. J., Heinrikson, R. L., & Law, J. H. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90671-x · Cited by 108 · see citing works
Apolipoprotein D is the major protein component in cyst fluid from women with human breast gross cystic disease
Balbı́n, M., Freije, J. M. P., Fueyo, A., Sánchez‐Pulido, L., & López-Otı́n, C. (1990) · Biochemical Journal · doi:10.1042/bj2710803 · Cited by 106 · 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
Electrophoretic Variation and Sex Dimorphism of the Major Urinary Protein Complex in Inbred Mice: A New Genetic Marker
Finlayson, J. S., Potter, M., & Runner, C. R. (1963) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/31.1.91 · Cited by 91 · see citing works
Primary Structure of Rat Brain Prostaglandin D Synthetase Deduced from cDNA Sequence
Urade, Y., Nagata, A., Suzuki, Y., Fujii, Y., & Hayaishi, O. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85050-0 · Cited by 89 · see citing works
Molecular mechanisms of olfaction.
Snyder, S. H., Sklar, P. B., & Pevsner, J. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68169-4 · Cited by 87 · see citing works
Structure of the epididymal retinoic acid binding protein at 2.1 Å resolution
Newcomer, M. E. (1993) · Structure · doi:10.1016/0969-2126(93)90004-z · Cited by 84 · see citing works
Regulation of a bifunctional mRNA results in synthesis of secreted and nuclear probasin.
Spence, A. M., Sheppard, P. C., Davie, J., Matuo, Y., Nishi, N., McKeehan, W. L., Dodd, J. G., & Matusik, R. J. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.20.7843 · Cited by 83 · see citing works
Possible pheromone‐carrier function of two lipocalin proteins in the vomeronasal organ.
Miyawaki, A., Matsushita, F., Ryo, Y., & Mikoshiba, K. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06927.x · Cited by 82 · see citing works
Sequence analysis, cellular localization, and expression of a neuroretina adhesion and cell survival molecule
Berman, P. W., Gray, P., Chen, E., Keyser, K. T., Ehrlich, D., Karten, H. J., LaCorbiere, M., Esch, F. S., & Schubert, D. A. (1987) · Cell · doi:10.1016/0092-8674(87)90018-3 · Cited by 82 · see citing works
Homology between the pyrazine‐binding protein from nasal mucosa and major urinary proteins
Cavaggioni, A., Sorbi, R. T., Keen, J. N., Pappin, D., & Findlay, J. B. C. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)81349-2 · Cited by 81 · see citing works
Protease-mediated signalling: new paradigms for cell regulation and drug development
Hollenberg, M. D. (1996) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(96)81562-8 · Cited by 80 · see citing works
The primary structure of aphrodisin.
Henzel, W. J., Rodriguez, H., Singer, A. G., Stults, J. T., Macrides, F., Agosta, W. C., & Niall, H. D. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37444-1 · Cited by 80 · see citing works
Apolipoprotein D transcription occurs specifically in nonproliferating quiescent and senescent fibroblast cultures
Provost, P. R., Marcel, Y. L., Milne, R. W., WEECH, P. K., & Rassart, É. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)81244-3 · Cited by 78 · see citing works
Apolipoprotein D gene induction by retinoic acid is concomitant with growth arrest and cell differentiation in human breast cancer cells.
López-Boado, Y. S., Tolivia, J., & López-Otı́n, C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47100-1 · Cited by 77 · see citing works
Internalization of retinol-binding protein in parenchymal and stellate cells of rat liver.
Senoo, H., Stang, E., Nilsson, A. C., Kindberg, G. M., Berg, T., Roos, N., Norum, K., & Blomhoff, R. (1990) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)42631-8 · Cited by 76 · 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
Characterization of disulfide-linked heterodimers containing apolipoprotein D in human plasma lipoproteins.
Blanco‐Vaca, F., Via, D. P., Yang, C., Massey, J., & Pownall, H. J. (1992) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)41336-7 · Cited by 76 · see citing works
Secretory endometrial and decidual proteins: studies and clinical significance of a maternally derived group of pregnancy-associated serum proteins
Bell, S. C. (1986) · Human Reproduction · doi:10.1093/oxfordjournals.humrep.a136369 · Cited by 75 · 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
Stimulation of apolipoprotein D secretion by steroids coincides with inhibition of cell proliferation in human LNCaP prostate cancer cells.
Simard, J., Veilleux, R., de Launoit, Y., Haagensen, D. E., & Labrie, F. (1991) · PubMed · Cited by 73 · see citing works
Ligand binding characteristics of homologous rat and mouse urinary proteins and pyrazine-binding protein of calf
Cavaggioni, A., Findlay, J. B. C., & Tirindelli, R. (1990) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(90)90049-y · Cited by 70 · see citing works
A chick neural retina adhesion and survival molecule is a retinol-binding protein.
Schubert, D. A., LaCorbiere, M., & Esch, F. S. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.102.6.2295 · Cited by 70 · see citing works
Intestinal uptake of retinol: enhancement by bovine milk beta-lactoglobulin
Said, H. M., Ong, D. E., & Shingleton, J. L. (1989) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/49.4.690 · Cited by 69 · see citing works
The architecture of invertebrate carotenoproteins
Zagalsky, P. F., Eliopoulos, E., & Findlay, J. B. C. (1990) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(90)90171-o · Cited by 69 · see citing works
[9] Invertebrate carotenoproteins
Zagalsky, P. F. (1985) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(85)11011-6 · Cited by 67 · see citing works
The mechanism of uptake of retinol by plasma-membrane vesicles.
Sivaprasadarao, A., & Findlay, J. B. C. (1988) · PubMed · Cited by 66 · see citing works
Tissue distribution of the receptor for plasma retinol-binding protein
Smeland, S., Bjerknes, T., Malaba, L. C., Eskild, W., Norum, K. R., & Blomhoff, R. (1995) · Biochemical Journal · doi:10.1042/bj3050419 · Cited by 66 · see citing works
Complete sequence and model for the A2 subunit of the carotenoid pigment complex, crustacyanin
Keen, J. N., CACERES, I., Eliopoulos, E., Zagalsky, P. F., & Findlay, J. B. C. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb15925.x · Cited by 66 · see citing works
Characteristics of chemical binding to α2u-globulin, in vitro—Evaluating structure-activity relationships
Borghoff, S. J., Miller, A. B., Bowen, J. P., & Swenberg, J. A. (1991) · Toxicology and Applied Pharmacology · doi:10.1016/0041-008x(91)90205-s · Cited by 63 · see citing works
Cloning and expression of human neutrophil lipocalin cDNA derived from bone marrow and ovarian cancer cells
Bartsch, S., & Tschesche, H. (1995) · FEBS Letters · doi:10.1016/0014-5793(94)01303-i · Cited by 63 · see citing works
Protein synthesis at the blood-brain barrier. The major protein secreted by amphibian choroid plexus is a lipocalin
Achen, M. G., Harms, P. J., Thomas, T., Richardson, S. J., Wettenhall, R. E. H., & Schreiber, G. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50072-7 · Cited by 62 · see citing works
Human α1‐microglobulin: Its measurement and clinical significance
Itoh, Y., & Kawai, T. (1990) · Journal of Clinical Laboratory Analysis · doi:10.1002/jcla.1860040511 · Cited by 62 · see citing works
Hematopoietic placental protein 14. An immunosuppressive factor in cells of the megakaryocytic lineage.
Morrow, D. M., Xiong, N., Getty, R. R., Ratajczak, M. Z., Morgan, D. A., Seppälä, M. T., Riittinen, L., Gewirtz, A. M., & Tykocinski, M. L. (1994) · PubMed Central · Cited by 61 · see citing works
Purification and crystallization of a retinoic acid-binding protein from rat epididymis. Identity with the major androgen-dependent epididymal proteins.
Newcomer, M. E., & Ong, D. E. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38241-9 · Cited by 60 · see citing works
The molecular organization of the protein HC-IgA complex (HC-IgA).
GRUBB, A. O., Méndez, E., Fernández-Luna, J. L., López, C., Mihaesco, E., & Vaerman, J. P. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67020-6 · Cited by 59 · see citing works
Three-dimensional arrangement of conserved amino acid residues in a superfamily of specific ligand-binding proteins
North, A. C. T. (1989) · International Journal of Biological Macromolecules · doi:10.1016/0141-8130(89)90041-x · Cited by 59 · see citing works
Rapid repression of quiescence-specific gene expression by epidermal growth factor, insulin, and pp60v-src.
Bédard, P., Yannoni, Y. M., Simmons, D. L., & Erikson, R. L. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.3.1371 · Cited by 58 · see citing works
Isolation of an adhesion-mediating protein from chick neural retina adherons.
Schubert, D. A., & LaCorbiere, M. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.3.1071 · Cited by 58 · see citing works
Isolation of a cell-surface receptor for chick neural retina adherons.
Schubert, D. A., & LaCorbiere, M. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.100.1.56 · Cited by 56 · see citing works
Developmental expression of the lipocalin Lazarillo and its role in axonal pathfinding in the grasshopper embryo
Sánchez, D., Ganfornina, M. D., & Bastiani, M. J. (1995) · Development · doi:10.1242/dev.121.1.135 · Cited by 54 · 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
Developmentally regulated synthesis of a low molecular weight protein (Ch 21) by differentiating chondrocytes.
Cancedda, F. D., Manduca, P., Tacchetti, C., Fossa, P., Quarto, R., & Cancedda, R. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.6.2455 · Cited by 52 · see citing works
Hormone and Age-Dependent Regulation of α2u-Globulin Gene Expression
Roy, A. K., Chatterjee, B., Demyan, W. F., Milin, B. S., Motwani, N. M., NATH, T. S., & Schiop, M. J. (1983) · Elsevier eBooks · doi:10.1016/b978-0-12-571139-5.50015-x · Cited by 51 · see citing works
Molecular mechanisms of olfaction
Snyder, S. H., Sklar, P. B., Hwang, P. M., & Pevsner, J. (1989) · Trends in Neurosciences · doi:10.1016/0166-2236(89)90154-9 · Cited by 48 · see citing works
Three‐dimensional structure and active site of three hydrophobic molecule‐binding proteins with significant amino acid sequence similarity
Monaco, H. L., & Zanotti, G. (1992) · Biopolymers · doi:10.1002/bip.360320425 · Cited by 48 · see citing works
Binding of ellipticine to β‐lactoglobulin
Dodin, G., Andrieux, M., & KABBANI, H. A. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19389.x · Cited by 46 · see citing works
Perireceptor Events in Taste
Schmale, H., Ahlers, C., Bläker, M., Kock, K., & Spielman, A. I. (2007) · Novartis Foundation symposium · doi:10.1002/9780470514511.ch11 · Cited by 45 · see citing works
Retinol-binding Protein and Asialo-orosomucoid Are Taken Up by Different Pathways in Liver Cells
Malaba, L. C., Smeland, S., Senoo, H., Norum, K. R., Berg, T., Blomhoff, R., & Kindberg, G. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.26.15686 · Cited by 44 · see citing works
Structure and Function of C8 in the Membrane Attack Sequence of Complement
Sodetz, J. M. (1988) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-73911-8_3 · Cited by 40 · see citing works
cDNA sequence and expression pattern of the putative pheromone carrier aphrodisin.
Mägert, H., Hadrys, T., Cieslak, A., Gröger, A., Feller, S. M., & Forssmann, W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.6.2091 · Cited by 36 · see citing works
The protein HC chromophore is linked to the cysteine residue at position 34 of the polypeptide chain by a reduction-resistant bond and causes the charge heterogeneity of protein HC
Escribano, J., GRUBB, A. O., Calero, M., & Méndez, E. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98474-7 · Cited by 35 · see citing works
Uterine endocrinology and paracrinology: insulin-like growth factor binding protein-1 and placental protein 14 revisited*
Seppälä, M. T., Koistinen, R. A., & Rutanen, E. ‐. (1994) · Human Reproduction · doi:10.1093/oxfordjournals.humrep.a138617 · Cited by 35 · see citing works
Isolation and characterization of fibronectin-α1-microglobulin complex in rat plasma
Falkenberg, C., Enghild, J. J., Thøgersen, I. B., Salvesen, G. S., & Åkerström, B. (1994) · Biochemical Journal · doi:10.1042/bj3010745 · Cited by 34 · see citing works
Identification of the protein HC receptor
Fernández-Luna, J. L., Leyva‐Cobián, F., & Mollinedo, F. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80079-6 · Cited by 34 · see citing works
Formation of the α1‐microglobulin chromophore in mammalian and insect cells: a novel post‐translational mechanism?
Åkerström, B., Bratt, T., & Enghild, J. J. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00206-o · Cited by 34 · see citing works
Lipocalin structure and function
Sivaprasadarao, A., Boudjelal, M., & Findlay, J. B. C. (1993) · Biochemical Society Transactions · doi:10.1042/bst0210619 · Cited by 34 · see citing works
The major androgen-regulated secretory proteins of the rat epididymis bear sequence homology with members of the alpha 2u-globulin superfamily.
Brooks, D. (1987) · PubMed · Cited by 34 · see citing works
LESP, an androgen-regulated lizard epididymal secretory protein family identified as a new member of the lipocalin superfamily
Morel, L., Dufaure, J. P., & Depeiges, A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82200-1 · Cited by 33 · see citing works
Structural and functional characterization of complement c8γ, a member of the lipocalin protein family
Haefliger, J., Peitsch, M. C., Jenne, D. E., & Tschopp, J. (1991) · Molecular Immunology · doi:10.1016/0161-5890(91)90095-2 · Cited by 33 · see citing works
The human lacrimal gland synthesizes apolipoprotein D mRNA in addition to tear prealbumin mRNA, both species encoding members of the lipocalin superfamily
Holzfeind, P. J., Merschak, P., Dieplinger, H., & Redl, B. (1995) · Experimental Eye Research · doi:10.1016/s0014-4835(05)80145-9 · Cited by 31 · see citing works
Structural homology of human complement component C8γ and plasma protein HC: Identity of the cysteine bond pattern
Haefliger, J., Jenne, D. E., Stanley, K. K., & Tschopp, J. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)90431-1 · Cited by 30 · see citing works
Binding of Retinol-binding Protein Obtained from Human Urine with Vitamin A Derivatives and Terpenoids
Hase, J., Kobashi, K., Nakai, N., & Onosaka, S. (1976) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a131080 · Cited by 29 · see citing works
Identification of genes differentially expressed in two types of v-myb-transformed avian myelomonocytic cells.
Nakano, T., & Graf, T. (1992) · PubMed · Cited by 29 · see citing works
The Complete Amino-Acid Sequence of the Bilin-Binding Protein fromPieris brassicaeand its Similarity to a Family of Serum Transport Proteins Like the Retinol-Binding Proteins
Suter, F., Kayser, H., & Zuber, H. (1988) · Biological Chemistry Hoppe-Seyler · doi:10.1515/bchm3.1988.369.1.497 · Cited by 28 · see citing works
Denatonium bitter tasting among transgenic mice expressing rat von Ebner's gland protein
Kock, K., Morley, S. D., Mullins, J. J., & Schmale, H. (1994) · Physiology & Behavior · doi:10.1016/0031-9384(94)90362-x · Cited by 27 · see citing works
Purification of human secretory pregnancy-associated endometrial α2-globulin (α2-PEG) from cytosol of first trimester pregnancy endometrium
Bell, S. C. (1986) · Human Reproduction · doi:10.1093/oxfordjournals.humrep.a136412 · Cited by 26 · see citing works
α1‐Microglobulin Glycopeptides Inhibit Antigen‐Specific Stimulation of Human Peripheral Blood Leucocytes
Åkerström, B., & Lögdberg, L. (1984) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.1984.tb01039.x · Cited by 24 · see citing works
The first prokaryotic lipocalins
Flower, D. R., Sansom, C., Beck, M. E., & Attwood, T. K. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)89116-1 · Cited by 23 · see citing works
Alpha1‐Microglobulin Is Mitogenic for Guinea Pig Lymphocytes
Lögdberg, L., Åkerström, B., & Shevach, E. M. (1986) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.1986.tb02173.x · Cited by 22 · see citing works
Mitogenic Effect of α1‐Microglobulin on Mouse Lymphocytes
Babiker-Mohamed, H., Åkerström, B., & Lögdberg, L. (1990) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.1990.tb02889.x · Cited by 21 · see citing works
The Homologous Species Restriction of the Complement Attack: Structure and Function of the C8 Binding Protein
Hänsch, G. M. (1988) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-73911-8_9 · Cited by 20 · see citing works
Alpha1-Microglobulin is Mitogenic to Human Peripheral Blood Lymphocytes. Regulation by both Enhancing and Suppressive Serum Factors
Babiker-Mohamed, H., Olsson, M. L., Boketoft, Å., Lögdberg, L., & Åkerström, B. (1990) · Immunobiology · doi:10.1016/s0171-2985(11)80330-x · Cited by 20 · see citing works
Identification of retinol as one of the protein HC chromophores
Escribano, J., GRUBB, A. O., & Méndez, E. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(88)81300-7 · Cited by 19 · see citing works
The pyrazine-binding protein and olfaction
Bignetti, E., Cattaneo, P., Cavaggioni, A., Damiani, G., & Tirindelli, R. (1988) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(88)90029-6 · Cited by 19 · see citing works
Characterization of Monoclonal Anti‐α1‐Microglobulin Antibodies: Binding Strength, Binding Sites, and Inhibition of Lymphocyte Stimulation
Babiker-Mohamed, H., Forsberg, M., Olsson, M. L., WINQUIST, O., Nilson, B., Lögdberg, L., & Åkerström, B. (1991) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.1991.tb01589.x · Cited by 16 · see citing works
Rapid Repression of Quiescence-Specific Gene Expression by Epidermal Growth Factor, Insulin, and pp60v-src
Bédard, P., Yannoni, Y. M., Simmons, D. L., & Erikson, R. L. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.3.1371-1375.1989 · Cited by 16 · see citing works
An increase in expression of the lipocalin 24p3 is found in mouse uterus coincident with birth
Kasik, J. W., & Rice, E. J. (1995) · American Journal of Obstetrics and Gynecology · doi:10.1016/0002-9378(95)90291-0 · Cited by 15 · see citing works
Changes of an androgen-dependent nuclear protein during functional differentiation and by dedifferentiation of the dorsolateral prostate of rats
Matuo, Y., Nishi, N., Tanaka, Y., Muguruma, Y., Tanaka, K., Akatsuka, Y., Matsui, S., Sandberg, A. A., & Wada, F. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)91326-3 · Cited by 15 · see citing works
α1-Microglobulin Destroys the Proteinase Inhibitory Activity of α1-Inhibitor-3 by Complex Formation
Falkenberg, C., Allhorn, M., Th⊘gersen, I. B., Valnickova, Z., Pizzo, S. V., Salvesen, G. S., Åkerström, B., & Enghild, J. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.9.4478 · Cited by 14 · see citing works
Role of alpha 1-microglobulin in immune response and inflammation.
Åkerström, B. (1992) · PubMed · Cited by 11 · see citing works
Improved ribbon-drawing programs
Flower, D. R. (1991) · Journal of Molecular Graphics · doi:10.1016/0263-7855(91)80021-q · Cited by 11 · see citing works
[38] α1-Acid glycoprotein
Arnaud, P., Miribel, L., & Roux, A. (1988) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(88)63040-0 · Cited by 11 · see citing works
The amino terminal sequence of the developmentally regulated Ch21 protein shows homology with amino terminal sequences of low molecular weight proteins binding hydrophobic molecules
Cancedda, F. D., Asaro, D., Molina, F., Cancedda, R., Caruso, C., Camardella, L., Negri, A. L., & Ronchi, S. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)91118-c · Cited by 10 · see citing works
Alpha 1-acid glycoprotein and peripheral nerve injury, studied with a wound chamber.
Liu, H., Hy, L., & Schmid, K. (1993) · PubMed · Cited by 4 · see citing works
FOLD: Integrated analysis and display of protein secondary structure
Flower, D. R. (1995) · Journal of Molecular Graphics · doi:10.1016/0263-7855(95)00072-0 · Cited by 3 · see citing works

Flagged first, then by citations

6 of the 148 references couldn’t be matched to a known paper.

Research works printed but not linked: 9

Sivaprasadarao, A., Boudjelal, M. and Findlay, J. B. C. (1993) Biochem. Soc. Trans. 21, 619-622
Goodman, W.S (1984) in The Retinoids (Sporn, M. B., Roberts, A. B. and Goodman, W. S, eds.), vol. 2, pp. 41-88, Academic Press, New York 40
Magert, H.-J., Hadrys, T., Cieslak, A., Groger, A., Feller, S. and Forssmann, W.-G. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 2091-2095
Pevsner, J., Trifiletti, R. R., Strittmatter, S. M. and Snyder, S. H. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 3050-3054
Nagata, A., Suzuki, Y., Igarashi, M., Eguchi, N., Toh, H., Urade, Y. and Hayaishi, O. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 4020-4024
Julkunen, M., Seppala, M. and Janne, O. A. (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 8845-8849 92
Mendez, E., Fernandez-Luna, J. L., Grubb, A. and Levy-Cobian (1986) Proc. Natl.Acad. Sci. U.S.A. 83, 3050-3054 101
Bennett, M. and Schmid, K. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 6109-6113 109
Spence, A. M., Sheppard, P. C., Davie, J. R., Matuo, Y., Nishi, N., McKeehan, W. L., Dodd, J. G. and Matusik, R. J. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 7843-7847 130

Sorted by citations

Granules of the Human Neutrophilic Polymorphonuclear Leukocyte
Borregaard, N., & Cowland, J. B. (1997) · Blood · doi:10.1182/blood.v89.10.3503 · Cited by 1,514 · see citing works
Soluble proteins in insect chemical communication
Pelosi, P., Zhou, J., Ban, L., & Calvello, M. A. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5607-0 · Cited by 876 · 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
Self-citation
Bovine β-lactoglobulin at 1.8 Å resolution — still an enigmatic lipocalin
Brownlow, S., Morais-Cabral, J. H., Cooper, R. A., Flower, D. R., Yewdall, S. J., Polikarpov, I., North, A. C. T., & Sawyer, L. (1997) · Structure · doi:10.1016/s0969-2126(97)00205-0 · Cited by 695 · see citing works
Role of Receptors in Bacillus thuringiensis Crystal Toxin Activity
Pigott, C. R., & Ellar, D. J. (2007) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00034-06 · Cited by 694 · see citing works
A Cell-Surface Receptor for Lipocalin 24p3 Selectively Mediates Apoptosis and Iron Uptake
Devireddy, L. R., Gazin, C., Zhu, X., & Green, M. R. (2005) · Cell · doi:10.1016/j.cell.2005.10.027 · Cited by 672 · see citing works
Scientific Opinion on the assessment of allergenicity of GM plants and microorganisms and derived food and feed
Panel), E. P. O. G. M. O. (. (2010) · EFSA Journal · doi:10.2903/j.efsa.2010.1700 · Cited by 610 · see citing works
Neutrophil Gelatinase–Associated Lipocalin (NGAL) as a Marker of Kidney Damage
Bolignano, D., Donato, V., Coppolino, G., Campo, S., Buemi, A., Lacquaniti, A., & Buemi, M. (2008) · American Journal of Kidney Diseases · doi:10.1053/j.ajkd.2008.01.020 · Cited by 591 · see citing works
Paracrine and endocrine actions of bone—the functions of secretory proteins from osteoblasts, osteocytes, and osteoclasts
Han, Y., You, X., Xing, W., Zhang, Z., & Zou, W. (2018) · Bone Research · doi:10.1038/s41413-018-0019-6 · Cited by 582 · see citing works
Structure and lipid transport mechanism of a StAR-related domain
Tsujishita (2000) · Nature Structural Biology · doi:10.1038/75192 · Cited by 535 · see citing works
New insights into the structure and function of fatty acid-binding proteins
Zimmerman, A. W., & Veerkamp, J. H. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-002-8490-y · Cited by 548 · see citing works
Identification of protein pheromones that promote aggressive behaviour
Chamero, P., Marton, T. F., Logan, D. W., Flanagan, K. A., Cruz, J. R., Saghatelian, A., Cravatt, B. F., & Stowers, L. (2007) · Nature · doi:10.1038/nature05997 · Cited by 529 · see citing works
Mammalian social odours: attraction and individual recognition
Brennan, P., & Kendrick, K. M. (2006) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2006.1931 · Cited by 510 · see citing works
Comparative Genomics of the Odorant-Binding and Chemosensory Protein Gene Families across the Arthropoda: Origin and Evolutionary History of the Chemosensory System
Vieira, F. G., & Rozas, J. (2011) · Genome Biology and Evolution · doi:10.1093/gbe/evr033 · Cited by 500 · see citing works
Biogenesis, molecular regulation and function of plant isoprenoids.
Bouvier, F., Rahier, A., & Camara, B. (2005) · Progress in Lipid Research · doi:10.1016/j.plipres.2005.09.003 · Cited by 498 · see citing works
The human fatty acid-binding protein family: Evolutionary divergences and functions
Smathers, R. L., & Petersen, D. R. (2011) · Human Genomics · doi:10.1186/1479-7364-5-3-170 · Cited by 493 · see citing works
Pheromonal communication in vertebrates
Brennan, P., & Zufall, F. (2006) · Nature · doi:10.1038/nature05404 · Cited by 485 · see citing works
Soluble proteins of chemical communication: an overview across arthropods
Pelosi, P., Iovinella, I., Felicioli, A., & Dani, F. R. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00320 · Cited by 479 · see citing works
The Adipokine Lipocalin 2 Is Regulated by Obesity and Promotes Insulin Resistance
Yan, Q.-W., Yang, Q., Mody, N., Graham, T. E., Hsu, C.-H., Xu, Z., Houstis, N. E., Kahn, B. B., & Rosen, E. D. (2007) · Diabetes · doi:10.2337/db07-0007 · Cited by 471 · 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
Retinoid-binding proteins: mediators of retinoid action
NOY, N. (2000) · Biochemical Journal · doi:10.1042/bj3480481 · Cited by 422 · see citing works
Retinoid-binding proteins: mediators of retinoid action
Noy, N. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3480481 · Cited by 420 · see citing works
Odorant-Binding Proteins in Insects
Zhou, J. (2010) · Vitamins and hormones · doi:10.1016/s0083-6729(10)83010-9 · Cited by 411 · 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
Induction of Apoptosis by a Secreted Lipocalin That is Transcriptionally Regulated by IL-3 Deprivation
Devireddy, L. R., Teodoro, J. G., Richard, F. A., & Green, M. R. (2001) · Science · doi:10.1126/science.1061075 · Cited by 379 · see citing works
Human neutrophil gelatinase-associated lipocalin and homologous proteins in rat and mouse
Kjeldsen, L., Cowland, J. B., & Borregaard, N. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00152-7 · Cited by 368 · see citing works
PNPLA3 has retinyl-palmitate lipase activity in human hepatic stellate cells
Pirazzi, C., Valenti, L. V. C., Motta, B. M., Pingitore, P., Hedfalk, K., Mancina, R. M., Burza, M. A., Indiveri, C., Ferro, Y., Montalcini, T., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu121 · Cited by 363 · see citing works
The Vomeronasal Organ Mediates Interspecies Defensive Behaviors through Detection of Protein Pheromone Homologs
Papes, F., Logan, D. W., & Stowers, L. (2010) · Cell · doi:10.1016/j.cell.2010.03.037 · Cited by 360 · see citing works
Neutrophil Gelatinase-Associated Lipocalin Is Up-Regulated in Human Epithelial Cells by IL-1β, but Not by TNF-α
Cowland, J. B., Sørensen, O. E., Sehested, M., & Borregaard, N. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.12.6630 · Cited by 354 · see citing works
The endocytic receptor megalin binds the iron transporting neutrophil‐gelatinase‐associated lipocalin with high affinity and mediates its cellular uptake
Hvidberg, V., Jacobsen, C. B., Strong, R. K., Cowland, J. B., Moestrup, S. K., & Borregaard, N. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.12.031 · Cited by 351 · 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
Biomarkers of Acute and Chronic Kidney Disease
Zhang, W. R., & Parikh, C. R. (2019) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020518-114605 · Cited by 336 · see citing works
Gene expression profiles in primary ovarian serous papillary tumors and normal ovarian epithelium: Identification of candidate molecular markers for ovarian cancer diagnosis and therapy
Santin, A. D., Zhan, F., Bellone, S., Palmieri, M., Canè, S., Bignotti, E., Anfossi, S., Gökden, M., Dunn, D. C., Roman, J. J., et al. (2004) · International Journal of Cancer · doi:10.1002/ijc.20408 · Cited by 314 · 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
The Role of Lipocalin 2 in the Regulation of Inflammation in Adipocytes and Macrophages
Zhang, J., Wu, Y., Zhang, Y., LeRoith, D., Bernlohr, D., & Chen, X. (2008) · Molecular Endocrinology · doi:10.1210/me.2007-0420 · Cited by 302 · see citing works
What's new in our understanding of the role of adipokines in rheumatic diseases?
Gómez, R., Conde, J., Scotece, M., Gómez-Reino, J. J., Lago, F., & Gualillo, O. (2011) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2011.107 · Cited by 300 · see citing works
Prostaglandin D synthase: Structure and function
Urade, Y., & Hayaishi, O. (2000) · Vitamins and hormones · doi:10.1016/s0083-6729(00)58022-4 · Cited by 295 · see citing works
Antimicrobial Activity of Mesenchymal Stem Cells: Current Status and New Perspectives of Antimicrobial Peptide-Based Therapies
Alcayaga‐Miranda, F., Cuenca, J., & Khoury, M. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00339 · Cited by 297 · see citing works
Mammalian odorant binding proteins
Tegoni, M., Pelosi, P., Vincent, F., Spinelli, S., Campanacci, V., Grolli, S., Ramoni, R., & Cambillau, C. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00167-9 · Cited by 280 · see citing works
The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity
Lehnert, N., Kim, E., Dong, H. T., Harland, J. B., Hunt, A. P., Manickas, E. C., Oakley, K. M., Pham, J., Reed, G. C., & Alfaro, V. S. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00253 · Cited by 277 · see citing works
Iron-withholding strategy in innate immunity
Ong, S. T., Shan Ho, J. Z., Ho, B., & Ding, J. L. (2006) · Immunobiology · doi:10.1016/j.imbio.2006.02.004 · Cited by 269 · see citing works
The Drosophila takeout Gene Is a Novel Molecular Link between Circadian Rhythms and Feeding Behavior
Sarov‐Blat, L., So, W. V., Liu, L., & Rosbash, M. (2000) · Cell · doi:10.1016/s0092-8674(00)80876-4 · Cited by 271 · 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
Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold
Beste, G., Schmidt, F. S., Stibora, T., & Skerra, A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.1898 · Cited by 268 · see citing works
Functional and Expression Pattern Analysis of Chemosensory Proteins Expressed in Antennae and Pheromonal Gland of Mamestra brassicae
Jacquin‐Joly, E. (2001) · Chemical Senses · doi:10.1093/chemse/26.7.833 · Cited by 265 · 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
Adipokines: New potential therapeutic target for obesity and metabolic, rheumatic, and cardiovascular diseases
Recinella, L., Orlando, G., Ferrante, C., Chiavaroli, A., Brunetti, L., & Leone, S. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.578966 · Cited by 261 · see citing works
Glycodelin: A Major Lipocalin Protein of the Reproductive Axis with Diverse Actions in Cell Recognition and Differentiation
Seppälä, M. T., Taylor, R. N., Koistinen, H. K., Koistinen, R., & Milgröm, E. (2002) · Endocrine Reviews · doi:10.1210/er.2001-0026 · Cited by 262 · see citing works
Nanobodies: Chemical Functionalization Strategies and Intracellular Applications
Schumacher, D., Helma, J., Schneider, A. F. L., Leonhardt, H., & Hackenberger, C. P. R. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201708459 · Cited by 261 · see citing works
Neutrophil Gelatinase-associated Lipocalin in Normal and Neoplastic Human Tissues. Cell Type-specific Pattern of Expression
Friedl, A., Stoesz, S. P., Buckley, P. J., & Gould, M. N. (1999) · The Histochemical Journal · doi:10.1023/a:1003708808934 · Cited by 260 · see citing works
Bovine milk allergenicity
Wal, J. M. (2004) · Annals of Allergy Asthma & Immunology · doi:10.1016/s1081-1206(10)61726-7 · Cited by 257 · see citing works
Identification of putative gene based markers of renal toxicity.
Amin, R. P., Vickers, A. E. M., Sistare, F. D., Thompson, K. L., Roman, R. J., Lawton, M. P., Kramer, J. A., Hamadeh, H. K., Collins, J. B., Grissom, S. F., et al. (2004) · Environmental Health Perspectives · doi:10.1289/ehp.6683 · Cited by 255 · 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
LUSH Odorant-Binding Protein Mediates Chemosensory Responses to Alcohols in Drosophila melanogaster
Kim, M.-S., Repp, A. B., & Smith, D. P. (1998) · Genetics · doi:10.1093/genetics/150.2.711 · Cited by 247 · see citing works
Siderocalin (Lcn 2) Also Binds Carboxymycobactins, Potentially Defending against Mycobacterial Infections through Iron Sequestration
Holmes, M. A., Paulsene, W., Jide, X., Ratledge, C., & Strong, R. K. (2005) · Structure · doi:10.1016/j.str.2004.10.009 · Cited by 246 · see citing works
Recombinant allergens for diagnosis and therapy of allergic disease
Chapman, M. D., Smith, A. M., Vailes, L. D., Arruda, L. K., Dhanaraj, V., & Pomés, A. (2000) · Journal of Allergy and Clinical Immunology · doi:10.1067/mai.2000.109832 · Cited by 246 · see citing works
The evolution of milk secretion and its ancient origins
Oftedal, O. T. (2011) · animal · doi:10.1017/s1751731111001935 · Cited by 242 · see citing works
Inflammation and metabolic dysfunction: links to cardiovascular diseases
Taube, A., Schlich, R., Sell, H., Eckardt, K., & Eckel, J. (2012) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00907.2011 · Cited by 239 · see citing works
Engineered protein scaffolds for molecular recognition
Skerra, A. (2000) · Journal of Molecular Recognition · doi:10.1002/1099-1352(200007/08)13:4 · Cited by 236 · see citing works
Increased protein backbone conformational entropy upon hydrophobic ligand binding.
Novotný, M. V., Stone, M. J., & Žı́dek, L. (1999) · Nature Structural Biology · doi:10.1038/70057 · Cited by 236 · see citing works
Proteins in urine scent marks of male house mice extend the longevity of olfactory signals
Hurst, J. L., Robertson, D. H. L., TOLLADAY, U., & Beynon, R. J. (1998) · Animal Behaviour · doi:10.1006/anbe.1997.0650 · Cited by 236 · see citing works
RBP4: a controversial adipokine
Kotnik, P., Fischer-Posovszky, P., & Wabitsch, M. (2011) · European Journal of Endocrinology · doi:10.1530/eje-11-0431 · Cited by 233 · see citing works
A review of carotenoid utilisation and function in crustacean aquaculture
Wade, N. M., Gabaudan, J., & Glencross, B. D. (2015) · Reviews in Aquaculture · doi:10.1111/raq.12109 · Cited by 233 · see citing works
NGAL: a biomarker of acute kidney injury and other systemic conditions
Soni, S. S., Cruz, D. N., Bobek, I., Chionh, C. Y., Nalesso, F., Lentini, P. L. M., de Cal, M., Corradi, V., Virzì, G. M., & Ronco, C. (2009) · International Urology and Nephrology · doi:10.1007/s11255-009-9608-z · Cited by 234 · see citing works
Something in the Air? New Insights into Mammalian Pheromones
Brennan, P. A., & Keverne, E. B. (2004) · Current Biology · doi:10.1016/j.cub.2003.12.052 · Cited by 236 · see citing works
Reducing the allergenic capacity of β-lactoglobulin by covalent conjugation with dietary polyphenols
Wu, X., Lu, Y., Xu, H., Lin, D., He, Z., Wu, H., Liu, L., & Wang, Z. (2018) · Food Chemistry · doi:10.1016/j.foodchem.2018.02.158 · Cited by 224 · see citing works
Positive identification of the puberty-accelerating pheromone of the house mouse: the volatile ligands associating with the major urinary protein
Novotný, M. V., Ma, W., Wiesler, D. P., & Žı́dek, L. (1999) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.1999.0880 · Cited by 219 · see citing works
Binding proteins from alternative scaffolds
Nygren, P., & Skerra, A. (2004) · Journal of Immunological Methods · doi:10.1016/j.jim.2004.04.006 · Cited by 218 · see citing works
Lipocalins as a scaffold
Skerra, A. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00145-x · Cited by 218 · see citing works
Neutrophil gelatinase-associated lipocalin (NGAL) is a predictor of poor prognosis in human primary breast cancer
Bauer, M., Eickhoff, J. C., Gould, M. N., Mundhenke, C., Maass, N., & Friedl, A. (2008) · Breast Cancer Research and Treatment · doi:10.1007/s10549-007-9619-3 · Cited by 215 · see citing works
Adaptation of ticks to a blood-feeding environment: evolution from a functional perspective
Mans, B. J., & Neitz, A. W. H. (2004) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2003.09.002 · Cited by 213 · see citing works
Complement Inhibitor of C5 Activation from the Soft Tick Ornithodoros moubata
Nunn, M. A., Sharma, A., Paesen, G. C., Adamson, S., Lissina, O., Willis, A. C., & Nuttall, P. A. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.4.2084 · Cited by 212 · see citing works
A new generation of protein display scaffolds for molecular recognition
Hosse, R. J., Rothe, A., & Power, B. E. (2005) · Protein Science · doi:10.1110/ps.051817606 · Cited by 211 · see citing works
Murine Pheromone Proteins Constitute a Context-Dependent Combinatorial Code Governing Multiple Social Behaviors
Kaur, A. W., Ackels, T., Kuo, T.-H., Cichy, A., Dey, S., Hays, C. K., Kateri, M., Logan, D. W., Marton, T. F., Spehr, M., et al. (2014) · Cell · doi:10.1016/j.cell.2014.02.025 · Cited by 207 · see citing works
Beetle immunity: Identification of immune-inducible genes from the model insect Tribolium castaneum
Altincicek, B., Knorr, E., & Vilcinskas, A. (2007) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2007.09.005 · Cited by 208 · 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
Lipocalins - a family portrait
Grzyb, J., Latowski, D., & Strzałka, K. (2006) · Journal of Plant Physiology · doi:10.1016/j.jplph.2005.12.007 · Cited by 205 · 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
Diverse functional roles of lipocalin-2 in the central nervous system
Jha, M. K., Lee, S., Park, D. H., Kook, H., Park, K.-G., Lee, I.-K., & Suk, K. (2015) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2014.12.006 · Cited by 195 · see citing works
Adipokines: Biofactors from white adipose tissue. A complex hub among inflammation, metabolism, and immunity
Conde, J., Scotece, M., Gómez, R., López, V., Gómez-Reino, J. J., Lago, F., & Gualillo, O. (2011) · BioFactors · doi:10.1002/biof.185 · Cited by 200 · see citing works
Cow's milk proteins/allergens
Wal, J. M. (2002) · Annals of Allergy Asthma & Immunology · doi:10.1016/s1081-1206(10)62115-1 · Cited by 200 · see citing works
Antimicrobial proteins and peptides: anti-infective molecules of mammalian leukocytes
Levy, O. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0604320 · Cited by 190 · see citing works
Structural Analysis and Disulfide-Bridge Pairing of Two Odorant-Binding Proteins from Bombyx mori
Scaloni, A., Monti, M., Angeli, S., & Pelosi, P. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1791 · Cited by 190 · see citing works
Proteomic Analysis of Cattle Tick Rhipicephalus (Boophilus) microplus Saliva: A Comparison between Partially and Fully Engorged Females
Tirloni, L., Reck, J., Terra, R. M. S., Martins, J. R., Mulenga, A., Sherman, N. E., Fox, J. W., Yates, J. R., Termignoni, C., Pinto, A. F. M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0094831 · Cited by 189 · see citing works
Isolation and characterization of human apolipoprotein M-containing lipoproteins
Christoffersen, C., Nielsen, L. B., Axler, O., Andersson, A., Johnsen, A. H., & Dahlbaäck, B. (2006) · Journal of Lipid Research · doi:10.1194/jlr.m600055-jlr200 · Cited by 188 · see citing works
Neutrophil gelatinase-associated lipocalin as a survival factor
Tong, Z., Wu, X., Ovcharenko, D., Zhu, J., Chen, C., & Kehrer, J. P. (2005) · Biochemical Journal · doi:10.1042/bj20051020 · Cited by 187 · see citing works
Molecular biology of insect olfaction:recent progress and conceptual models
Rützler, M. R., & Zwiebel, L. J. (2005) · Journal of Comparative Physiology A · doi:10.1007/s00359-005-0044-y · Cited by 188 · see citing works
Secreted Wingless-interacting molecule (Swim) promotes long-range signaling by maintaining Wingless solubility
Mulligan, K. A., Fuerer, C., Ching, W., Fish, M., Willert, K., & Nusse, R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1119197109 · Cited by 187 · see citing works
X-ray Structure and Ligand Binding Study of a Moth Chemosensory Protein
Lartigue, A., Campanacci, V., Roussel, A., Larsson, A. M., Jones, T. A., Tegoni, M., & Cambillau, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204371200 · Cited by 186 · see citing works
Targeting the hepcidin–ferroportin axis to develop new treatment strategies for anemia of chronic disease and anemia of inflammation
Sun, C. C., Vaja, V., Babitt, J. L., & Lin, H. Y.-F. (2011) · American Journal of Hematology · doi:10.1002/ajh.23110 · Cited by 181 · see citing works
Cow's milk allergens
Wal, J. M. (1998) · Allergy · doi:10.1111/j.1398-9995.1998.tb03811.x · Cited by 185 · see citing works
Ligand Preference Inferred from the Structure of Neutrophil Gelatinase Associated Lipocalin
Goetz, D. H., Willie, S. T., Armen, R. S., Bratt, T., Borregaard, N., & Strong, R. K. (2000) · Biochemistry · doi:10.1021/bi992215v · Cited by 184 · see citing works
Effect of Heat Treatment on the Conformation and Aggregation of β-Lactoglobulin A, B, and C
Manderson, G. A., Hardman, M. J., & Creamer, L. K. (1998) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf980515y · Cited by 183 · see citing works
Adipokines: Linking metabolic syndrome, the immune system, and arthritic diseases
Francisco, V., Ruiz‐Fernández, C., Pino, J., Mera, A., González-Gay, M. Á., Gómez, R., Lago, F., Mobasheri, A., & Gualillo, O. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.03.030 · Cited by 182 · see citing works
Comparative analysis of Klebsiella pneumoniae genomes identifies a phospholipase D family protein as a novel virulence factor
Lery, L. M., Frangeul, L., Tomas, A., Passet, V., Almeida, A. S., Bialek-Davenet, S., Barbe, V., Bengoechea, J. A., Sansonetti, P., Brisse, S., et al. (2014) · BMC Biology · doi:10.1186/1741-7007-12-41 · Cited by 181 · see citing works
From the periphery to the brain: Lipocalin-2, a friend or foe?
Ferreira, A. C., Mesquita, S. D., Sousa, J. C., Correia‐Neves, M., Sousa, N., Palha, J. A., & Marques, F. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.06.005 · Cited by 174 · see citing works
Structural Basis of Multidrug Recognition by BmrR, a Transcription Activator of a Multidrug Transporter
Heldwein, E. E. Z., Markham, P. N., Neyfakh, A. A., & Brennan, R. G. (1999) · Cell · doi:10.1016/s0092-8674(00)80548-6 · Cited by 177 · see citing works
Identification of a putative lysosomal cobalamin exporter altered in the cblF defect of vitamin B12 metabolism
Rutsch, F., Gailus, S., Miousse, I. R., Suormala, T., Sagné, C., Toliat, M. R., Nürnberg, G., Wittkampf, T., Buers, I., Sharifi, A., et al. (2009) · Nature Genetics · doi:10.1038/ng.294 · Cited by 177 · see citing works
A review of the molecular mechanisms of acaricide resistance in mites and ticks
Rouck, S. D., İnak, E., Dermauw, W., & Leeuwen, T. V. (2023) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2023.103981 · Cited by 177 · see citing works

Authors: FLOWER, D. R.
Affiliations: Department of Physical Chemistry and BioAnalysis, Astra Charnwood, Bakewell Road, Loughborough, Leics. LE11 5RH, U.K.
Corresponding author: FLOWER, Darren R.
ORCID: FLOWER, Darren R.
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 1996-08-15
Volume: 318
Issue: 1
Pages: 1-14
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj3180001
PMC: PMC1217580
OpenAlex: W2040141270
Cited by: 1,679
References: 148
Citations by year: 2026: 24 · 2025: 33 · 2024: 41 · 2023: 53 · 2022: 49 · 2021: 64 · 2020: 68 · 2019: 51 · 2018: 43 · 2017: 53 · 2016: 69 · 2015: 73 · 2014: 79 · 2013: 81 · 2012: 91
FWCI: 3.93
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords: lipocalin, protein structure, beta-barrel, ligand-binding proteins, fatty acid binding protein, avidin, retinol transport, cryptic coloration, olfaction, prostaglandin synthesis, cell surface receptors, membrane transporters, immune regulation
MeSH terms: Adjuvants, Immunologic, Amino Acid Sequence, Avidin, Carrier Proteins, Ligands, Models, Molecular, Molecular Sequence Data, Neoplasm Proteins, Pheromones, Protein Binding, Proteins, Receptors, Cell Surface, Smell, Myelin P2 Protein, Fatty Acid-Binding Proteins

About these checks

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

Statistics and arithmetic are recomputed, not judged.

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

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

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

The lipocalin protein family: structure and function

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks