The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
The lipocalin protein family: structural and sequence overview
Abstract
Lipocalins are remarkably diverse at the sequence level yet have highly conserved structures. Most lipocalins share three characteristic conserved sequence motifs - the kernel lipocalins - while others are more divergent family members - the outlier lipocalins - typically sharing only one or two. This classification is a useful tool for analysing the family, and within these large sets are smaller groups sharing much higher levels of sequence similarity. The lipocalins are also part of a larger protein superfamily: the calycins, which includes the fatty acid binding proteins, avidins, a group of metalloproteinase inhibitors, and triabin. The superfamily is characterised by a similar structure (a repeated +1 topology beta-barrel) and by the conservation of a remarkable structural signature.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“The ADAM (A Disintegrin And Metalloprotease) and ADAMTS families of metalloproteases are encoded by over 40 human genes, mediate cell-cell and cell-matrix interactions (20, 21) and are involved in a range of human diseases, including cancer metastasis, inflammatory disorders, neurological diseases and asthma (21, 22).”
From Accurate prediction of protein structures and interactions using a 3-track network (2021) · cites this paper as [20]
Citations
Cites
Murzin, A. G., Brenner, S. E., Hubbard, T., & Chothia, C. (1995) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80134-2 · Cited by 6,445
The lipocalin protein family: structure and function
FLOWER, D. R. (1996) · Biochemical Journal · doi:10.1042/bj3180001 · Cited by 1,679
Self-citationThe PROSITE database, its status in 1999
Hofmann, K., Bücher, P., Falquet, L., & Bairoch, A. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.1.215 · Cited by 1,092
Green, N. M. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)84259-j · Cited by 1,020
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 714
Self-citationLipid-Binding Proteins: A Family of Fatty Acid and Retinoid Transport Proteins
Banaszak, L. J., Winter, N. S., Xu, Z., Bernlohr, D., Cowan, S. W., & Jones, A. T. (1994) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60639-7 · Cited by 483
Borgstahl, G. E. O., Williams, D. R., & Getzoff, E. D. (1995) · Biochemistry · doi:10.1021/bi00019a004 · Cited by 438
Harpaz, Y., & Chothia, C. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1312 · Cited by 435
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
Self-citationStructure 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
Self-citation
Cited by
Sorted by citations
Items 101–200 of 867
Novel Biomarkers of Heart Failure
Savic-Radojevic, A. R., Pljesa-Ercegovac, M. S., Matic, M., Simic, D., Radovanović, S., & Simic, T. P. (2016) · Advances in clinical chemistry · doi:10.1016/bs.acc.2016.09.002 · Cited by 113
Gentamicin induced acute renal damage and its evaluation using urinary biomarkers in rats
Udupa, V., & Prakash, V. (2018) · Toxicology Reports · doi:10.1016/j.toxrep.2018.11.015 · Cited by 111
Structure, Function, and Evolution of Biogenic Amine-binding Proteins in Soft Ticks
Mans, B. J., Ribeiro, J. M. C., & Andersen, J. F. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800188200 · Cited by 110
Cellular and mitochondrial iron homeostasis in vertebrates
Chen, C., & Paw, B. H. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.01.003 · Cited by 111
Temperature‐induced lipocalin is required for basal and acquired thermotolerance in Arabidopsis
Chi, W.-T., Fung, R. W. M., Liu, H., HSU, C., & Charng, Y. (2009) · Plant Cell & Environment · doi:10.1111/j.1365-3040.2009.01972.x · Cited by 107
FIBRILLIN4Is Required for Plastoglobule Development and Stress Resistance in Apple and Arabidopsis
Singh, D. K., Maximova, S. N., Jensen, P. J., Lehman, B. L., Ngugi, H. K., & McNellis, T. W. (2010) · PLANT PHYSIOLOGY · doi:10.1104/pp.110.164095 · Cited by 107
Pan, F., Li, J., Zhao, L., Tuersuntuoheti, T., Mehmood, A., Zhou, N., Hao, S., Wang, C., Guo, Y., & Lin, W. (2020) · Journal of Food Biochemistry · doi:10.1111/jfbc.13570 · Cited by 108
Playford, R. J., Belo, A., Poulsom, R., Fitzgerald, A. J., Harris, K. M., Pawluczyk, I., Ryon, J., Darby, T., Nilsen‐Hamilton, M., Ghosh, S. K., et al. (2006) · Gastroenterology · doi:10.1053/j.gastro.2006.05.051 · Cited by 105
Lovelace, L. L., Cooper, C. L., Sodetz, J. M., & Lebioda, L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.219766 · Cited by 105
Structural dynamics and folding of β-lactoglobulin probed by heteronuclear NMR
Sakurai, K., Konuma, T., Yagi, M., & Goto, Y. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.04.003 · Cited by 108
Apolipoprotein D in lipid metabolism and its functional implication in atherosclerosis and aging
Perdomo, G., & Dong, H. H. (2008) · Aging · doi:10.18632/aging.100004 · Cited by 110
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
Aigner, F., Maier, H., Schwelberger, H. G., Wallnöfer, E. A., Amberger, A., Obrist, P., Berger, T., Mak, T. W., Maglione, M., Margreiter, R., et al. (2007) · American Journal of Transplantation · doi:10.1111/j.1600-6143.2006.01723.x · Cited by 102
Berry, D. C., & Noy, N. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2011.07.002 · Cited by 100
An insight into the sialotranscriptome of the brown dog tick, Rhipicephalus sanguineus
Anatriello, E., Ribeiro, J. M. C., Santos, I. K. F. D. M., Brandão, L. G., Anderson, J. M., Valenzuela, J. G., Maruyama, S. R., Silva, J. S., & Ferreira, B. R. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-450 · Cited by 98
Lipocalin-2 is involved in emotional behaviors and cognitive function
Ferreira, A. C. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00122 · Cited by 99
Neutrophil Gelatinase-associated Lipocalin Acts as a Protective Factor against H2O2 Toxicity
Roudkenar, M. H., Halabian, R., Ghasemipour, Z., Roushandeh, A. M., Rouhbakhsh, M., Nekogoftar, M., Kuwahara, Y., Fukumoto, M., & Shokrgozar, M. A. (2008) · Archives of Medical Research · doi:10.1016/j.arcmed.2008.05.003 · Cited by 97
Berger, T., Cheung, C. C., Elia, A. J., & Mak, T. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000101107 · Cited by 96
Hofmann, E., Zerbe, P., & Schaller, F. (2006) · The Plant Cell · doi:10.1105/tpc.106.043984 · Cited by 96
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
Francischetti, I. M. B., Meng, Z., Mans, B. J., Gudderra, N. P., Hall, M. R., Veenstra, T. D., Pham, V. M., Kotsyfakis, M., & Ribeiro, J. M. C. (2008) · Journal of Proteomics · doi:10.1016/j.jprot.2008.07.006 · Cited by 95
Lipocalin 2 as a link between ageing, risk factor conditions and age-related brain diseases
Dekens, D. W., Eisel, U. L. M., Gouweleeuw, L., Schoemaker, R. G., Deyn, P. P. D., & Naudé, P. J. W. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101414 · Cited by 93
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
Astashkina, A. I., Mann, B. K., Prestwich, G. D., & Grainger, D. W. (2012) · Biomaterials · doi:10.1016/j.biomaterials.2012.03.001 · Cited by 93
Current developments in early diagnosis of acute kidney injury
Obermüller, N., Geiger, H., Weipert, C., & Urbschat, A. (2013) · International Urology and Nephrology · doi:10.1007/s11255-013-0448-5 · Cited by 92
Plasma fatty acid binding protein 4 is associated with atherogenic dyslipidemia in diabetes
Cabré, A., Lázaro, I., Girona, J., Manzanares, J. M., Marimón, F., Plana, N., Heras, M., & Masana, L. (2008) · Journal of Lipid Research · doi:10.1194/jlr.m800102-jlr200 · Cited by 91
Retinol-binding protein 4 in obesity and metabolic dysfunctions
Nankam, P. A. N., & Blüher, M. (2021) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2021.111312 · Cited by 93
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 96
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 92
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
Rhizavidin from Rhizobium etli: the first natural dimer in the avidin protein family
Helppolainen, S. H., Nurminen, K. P., Määttä, J. A. E., Halling, K. K., Slotte, J. P., Huhtala, T., Liimatainen, T., Ylä‐Herttuala, S., Airenne, K. J., Närvänen, A. T. O., et al. (2007) · Biochemical Journal · doi:10.1042/bj20070076 · Cited by 89
Effect of protein–surfactant interactions on aggregation of β-lactoglobulin
Hansted, J. G., Wejse, P. L., Bertelsen, H., & Otzen, D. E. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.03.011 · Cited by 89
The sialotranscriptome of the blood-sucking bug Triatoma brasiliensis (Hemiptera, Triatominae)
Santos, A. R., Ribeiro, J. M. C., Lehane, M. J., Gontijo, N. F., Veloso, A. B., Sant'Anna, M. R. V., Araújo, R. N., Grisard, E. C., & Pereira, M. H. (2007) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2007.04.004 · Cited by 88
Hilger, C., Kuehn, A., & Hentges, F. (2012) · Current Allergy and Asthma Reports · doi:10.1007/s11882-012-0283-2 · Cited by 86
A Strategy for Discovery of Endocrine Interactions with Application to Whole-Body Metabolism
Seldin, M. M., Koplev, S., Rajbhandari, P., Vergnes, L., Rosenberg, G. M., Meng, Y., Pan, C., Phuong, T. M. N., Gharakhanian, R., Che, N., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.03.015 · Cited by 84
Willis, J. H., Papandreou, N. C., Iconomidou, V. A., & Hamodrakas, S. J. (2011) · Elsevier eBooks · doi:10.1016/b978-0-12-384747-8.10005-4 · Cited by 84
Efflux-mediated drug resistance in Gram-positive bacteria
Markham, P. N. (2001) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(00)00243-5 · Cited by 84
Principles of odor coding in vertebrates and artificial chemosensory systems
Manzini, I., Schild, D., & Natale, C. D. (2021) · Physiological Reviews · doi:10.1152/physrev.00036.2020 · Cited by 90
Dyer, D. H., Lovell, S., Thoden, J. B., Holden, H. M., Rayment, I., & Lan, Q. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306214200 · Cited by 83
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
Social interactions affecting caste development through physiological actions in termites
Watanabe, D., Gotoh, H., Miura, T., & Maekawa, K. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00127 · Cited by 82
Bile salt receptor complex activates a pathogenic type III secretion system
Li, P., Rivera‐Cancel, G., Kinch, L. N., Salomon, D., Tomchick, D. R., Grishin, N. V., & Orth, K. (2016) · eLife · doi:10.7554/elife.15718 · Cited by 81
Mans, B. J. (2003) · Molecular Biology and Evolution · doi:10.1093/molbev/msg126 · Cited by 81
Toyonaga, T., Matsuura, M., Mori, K., Honzawa, Y., Minami, N., Yamada, S., Kobayashi, T., Hibi, T., & Nakase, H. (2016) · Scientific Reports · doi:10.1038/srep35014 · Cited by 75
Engineering adipic acid metabolism in Pseudomonas putida
Ackermann, Y. S., Li, W., de Hipt, L. O., Niehoff, P.-J., Casey, W. T., Polen, T., Köbbing, S., Ballerstedt, H., Wynands, B., O’Connor, K. E., et al. (2021) · Metabolic Engineering · doi:10.1016/j.ymben.2021.05.001 · Cited by 82
Dirigent proteins: molecular characteristics and potential biotechnological applications
Pickel, B., & Schaller, A. (2013) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-013-5167-4 · Cited by 80
Lipocalin 2: a potential therapeutic target for breast cancer metastasis
Hu, C., Yang, K., Li, M., Huang, W., Zhang, F., & Wang, H. (2018) · OncoTargets and Therapy · doi:10.2147/ott.s181223 · Cited by 80
A role of apolipoprotein D in triglyceride metabolism
Perdomo, G., Kim, D. H., Zhang, T., Qu, S., Thomas, E. A., Toledo, F. G. S., Slusher, S., Fan, Y., Kelley, D. E., & Dong, H. H. (2010) · Journal of Lipid Research · doi:10.1194/jlr.m001206 · Cited by 78
Polymorphism in Major Urinary Proteins: Molecular Heterogeneity in a Wild Mouse Population
Beynon, R. J., Veggerby, C., Payne, C. E., Robertson, D. H. L., Gaskell, S. J., Humphries, R. E., & Hurst, J. L. (2002) · Journal of Chemical Ecology · doi:10.1023/a:1016252703836 · Cited by 78
Across intra-mammalian stages of the liver f luke Fasciola hepatica: a proteomic study
Maggio, L. S. D., Tirloni, L., Pinto, A. F. M., Diedrich, J. K., Yates, J. R., Benavides, U., Carmona, C., Vaz, I. D. S., & Berasain, P. (2016) · Scientific Reports · doi:10.1038/srep32796 · Cited by 77
Deamidated Lipocalin‐2 Induces Endothelial Dysfunction and Hypertension in Dietary Obese Mice
Song, E., Fan, P., Huang, B., Deng, H., Cheung, B. M. Y., Félétou, M., Vilaine, J., Villeneuve, N., Xu, A., Vanhoutte, P. M., et al. (2014) · Journal of the American Heart Association · doi:10.1161/jaha.114.000837 · Cited by 77
Genome-Mined Diels–Alderase Catalyzes Formation of the cis-Octahydrodecalins of Varicidin A and B
Tan, D., Jamieson, C. S., Ōhashi, M., Tang, M., Houk, K. N., & Tang, Y. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b12010 · Cited by 77
Adam, B., Charloteaux, B., Beaufays, J., Vanhamme, L., Godfroid, E., Brasseur, R., & Lins, L. (2008) · BMC Structural Biology · doi:10.1186/1472-6807-8-1 · Cited by 77
Wang, Y. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01528.x · Cited by 75
Odorant Binding and Conformational Changes of a Rat Odorant-binding Protein
Nespoulous, C. (2004) · Chemical Senses · doi:10.1093/chemse/bjh017 · Cited by 74
Wojnar, P., Lechner, M., Merschak, P., & Redl, B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101762200 · Cited by 73
Slade, D. J., Lovelace, L. L., Chruszcz, M., Minor, W., Lebioda, L., & Sodetz, J. M. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.03.061 · Cited by 73
Aphrodisin, an aphrodisiac lipocalin secreted in hamster vaginal secretions.
Briand, L., Trotier, D., & Pernollet, J. (2004) · Peptides · doi:10.1016/j.peptides.2003.10.026 · Cited by 64
Relationships of lipocalin 2 with breast tumorigenesis and metastasis
Leng, X., Wu, Y., & Arlinghaus, R. B. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22403 · Cited by 72
Omics analysis reveals variations among commercial sources of bovine milk fat globule membrane
Brink, L., Herren, A. W., McMillen, S. A., Fraser, K., Agnew, M. P., Roy, N. C., & Lönnerdal, B. L. (2020) · Journal of Dairy Science · doi:10.3168/jds.2019-17179 · Cited by 72
Madhurantakam, C., Nilsson, O. B., Uchtenhagen, H., Konradsen, J. R., Saarne, T., Högbom, E., Sandalova, T., Grönlund, H., & Achour, A. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.05.043 · Cited by 70
Neutrophil gelatinase-associated lipocalin: new paths for an old shuttle.
Devarajan, P. (2007) · PubMed · Cited by 70
Andersen, J. F., Gudderra, N. P., Francischetti, I. M. B., Valenzuela, J. G., & Ribeiro, J. M. C. (2004) · Biochemistry · doi:10.1021/bi049655t · Cited by 70
New Biomarkers of Acute Kidney Injury and the Cardio-renal Syndrome
Hawkins, R. C. (2011) · Annals of Laboratory Medicine · doi:10.3343/kjlm.2011.31.2.72 · Cited by 69
Xiao, Y., Xu, A., Hui, X. H., Zhou, P., Li, X., Zhong, H., Tang, W., Huang, G., & Zhou, Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066607 · Cited by 70
Solution structure of a chemosensory protein from the moth Mamestra brassicae
Mosbah, A., Campanacci, V., Lartigue, A., Tegoni, M., Cambillau, C., & Darbon, H. (2002) · Biochemical Journal · doi:10.1042/bj20021217 · Cited by 67
Mechanistic biomarkers for cytotoxic acute kidney injury
Vaidya, V. S., & Bonventre, J. V. (2006) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1517/17425255.2.5.697 · Cited by 66
Zsila, F., Hazai, E., & Sawyer, L. (2005) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf051944g · Cited by 67
Overview of Protein Structural and Functional Folds
Sun, P. D., Foster, C. E., & Boyington, J. C. (2004) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps1701s35 · Cited by 80
Altered bone development and turnover in transgenic mice over‐expressing Lipocalin‐2 in bone
Costa, D., Lazzarini, E., Canciani, B., Giuliani, A., Spanò, R., Marozzi, K., Mănescu, A., Cancedda, R., & Tavella, S. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24391 · Cited by 66
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
Antimicrobial activity of bovine β-lactoglobulin against mastitis-causing bacteria
Chaneton, L., Sáez, J. M. P., & Bussmann, L. E. (2010) · Journal of Dairy Science · doi:10.3168/jds.2010-3319 · Cited by 65
Odorant‐binding proteins of mammals
Pelosi, P., & Knoll, W. (2021) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12787 · Cited by 64
Emerging clinical and experimental evidence for the role of lipocalin‐2 in metabolic syndrome
Jang, Y., Lee, J. H., Wang, Y., & Sweeney, G. (2011) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2011.05557.x · Cited by 64
Structural Characterization of the Type-III Pilot-Secretin Complex from Shigella flexneri
Okon, M., Moraes, T. F., Lario, P. I., Creagh, A. L., Haynes, C. A., Strynadka, N. C. J., & McIntosh, L. P. (2008) · Structure · doi:10.1016/j.str.2008.08.006 · Cited by 64
Douglas, T., Vandrovcová, M., Kročilová, N., Keppler, J. K., Zárubová, J., Skirtach, A. G., & Bačáková, L. (2017) · Journal of Dairy Science · doi:10.3168/jds.2017-13119 · Cited by 64
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
Structural and Functional Analysis of Tetracenomycin F2 Cyclase from Streptomyces glaucescens
Thompson, T. B., Katayama, K., Watanabe, K., Hutchinson, C. R., & Rayment, I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406144200 · Cited by 63
Lim, D., Jeong, J., & Song, J. (2021) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13653 · Cited by 64
Roudkenar, M. H., Halabian, R., Roushandeh, A. M., Nourani, M. R., Masroori, N., Ebrahimi, M., Nikogoftar, M., Rouhbakhsh, M., Bahmani, P., Jahanian‐Najafabadi, A., et al. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2009.08.019 · Cited by 62
Structure, Functions, and Physiological Roles of the Lipocalin α1-Microglobulin (A1M)
Bergwik, J., Kristiansson, A., Allhorn, M., Gram, M., & Åkerström, B. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.645650 · Cited by 61
Lipocalin-2 (LCN2) regulates PLIN5 expression and intracellular lipid droplet formation in the liver
Asimakopoulou, A., Borkham‐Kamphorst, E., Henning, M., Yagmur, E., Gaßler, N., Liedtke, C., Berger, T., Mak, T. W., & Weiskirchen, R. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.07.017 · Cited by 61
Wang, Q., Li, S., Tang, X., Li, L., Wang, F., & Du, H. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02594 · Cited by 64
Shashidharamurthy, R., Machiah, D. K., Aitken, J. D., Putty, K., Srinivasan, G., Chassaing, B., Parkos, C. A., Selvaraj, P., & Vijay–Kumar, M. (2012) · Arthritis & Rheumatism · doi:10.1002/art.37840 · Cited by 60
Zsila, F., Bikádi, Z., & Simonyi, M. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01350-3 · Cited by 60
Sahihi, M., & Ghayeb, Y. (2014) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2014.04.022 · Cited by 60
Linking iron-deficiency with allergy: role of molecular allergens and the microbiome
Roth‐Walter, F., Pacios, L. F., Bianchini, R., & Jensen‐Jarolim, E. (2017) · Metallomics · doi:10.1039/c7mt00241f · Cited by 61
Analysis of fat body transcriptome from the adult tsetse fly, Glossina morsitans morsitans
Attardo, G. M., Strickler-Dinglasan, P., Perkin, S. A. H., Caler, E. V., Bonaldo, M. F., Soares, M. B., El‐Sayeed, N., & Aksoy, S. (2006) · Insect Molecular Biology · doi:10.1111/j.1365-2583.2006.00649.x · Cited by 60
Campanacci, V., Bishop, R. E., Blangy, S., Tegoni, M., & Cambillau, C. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.07.086 · Cited by 59
Sexual differences in the sialomes of the zebra tick, Rhipicephalus pulchellus
Tan, A. W. L., Francischetti, I. M. B., Slovák, M., Kini, R. M., & Ribeiro, J. M. C. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2014.12.014 · Cited by 61
Wiederstein, M., & Sippl, M. J. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.11.012 · Cited by 59
Stone, C. E., Hall, D. H., & Sundaram, M. V. (2009) · Developmental Biology · doi:10.1016/j.ydbio.2009.02.030 · Cited by 58
Barasch, J. M., & Mori, K. (2004) · Nature · doi:10.1038/432811a · Cited by 59
Song, J., & Kim, O. Y. (2018) · Clinical Nutrition Research · doi:10.7762/cnr.2018.7.1.1 · Cited by 53
Assessment of recombinant dog allergens Can f 1 and Can f 2 for the diagnosis of dog allergy
Saarelainen, S., Taivainen, A., Rytkönen‐Nissinen, M., Auriola, S., Immonen, A., Mäntyjärvi, R., Rautiainen, J., Kinnunen, T., & Virtanen, T. (2004) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2004.02071.x · Cited by 59
Asaf, S., Maqsood, F., Jalil, J., Sarfraz, Z., Sarfraz, A., Mustafa, S., & Chérrez-Ojeda, I. (2022) · Immunologic Research · doi:10.1007/s12026-022-09352-2 · Cited by 58
The pivotal role played by lipocalin-2 in chronic inflammatory pain
Jha, M. K., Jeon, S., Jin, M., Ock, J., Kim, J.-H., Lee, W., & Suk, K. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2014.01.009 · Cited by 58
Sahihi, M., Heidari-Koholi, Z., & Bordbar, A.-K. (2012) · Journal of Macromolecular Science Part B · doi:10.1080/00222348.2012.672854 · Cited by 58
Human plasma retinol-binding protein (RBP4) is also a fatty acid-binding protein
Perduca, M., Nicolis, S., Mannucci, B., Galliano, M., & Monaco, H. L. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2018.01.010 · Cited by 57
Biomarkers of acute kidney injury
Peres, L. A. B., Júnior, A. D. D. C., Schäfer, A. J., da Silva, A. L., Gaspar, A. D., Scarpari, D. F., Alves, J. B. F., Neto, R. G., & de Oliveira, T. F. T. (2013) · Brazilian Journal of Nephrology · doi:10.5935/0101-2800.20130036 · Cited by 57
Metadata
- Authors
- Flower, D. R., North, A. C. T., & Sansom, C. E.
- Affiliations
- Jenner Institute (GB)
- University of Leeds (GB)
- University of London (GB)
- Corresponding author
- Flower, Darren R.
- ORCID
- Flower, Darren R.
- Venue
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Publisher
- Elsevier BV
- Published
- 2000-10
- Volume
- 1482
- Issue
- 1-2
- Pages
- 9-24
- ISSN
- 0167-4838 (ISSN-L)
- OpenAlex
- W2038438679
- Cited by
- 868
- References
- 59
- Citations by year
- 2026: 18 · 2025: 26 · 2024: 25 · 2023: 27 · 2022: 29 · 2021: 33 · 2020: 37 · 2019: 27 · 2018: 29 · 2017: 35 · 2016: 46 · 2015: 39 · 2014: 51 · 2013: 37 · 2012: 60
- FWCI
- 1.34
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology (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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- lipocalin, protein superfamilies, conserved motifs, fatty acid binding protein, avidin, metalloproteinase inhibitors, protein structure conservation
- MeSH terms
- Fatty Acid-Binding Protein 7, Amino Acid Sequence, Animals, Carrier Proteins, Humans, Lactoglobulins, Models, Molecular, Molecular Sequence Data, Neoplasm Proteins, Protein Conformation, Sequence Homology, Amino Acid, Insect Proteins, Tumor Suppressor Proteins, 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