The DOI matches its Crossref record; 142 of the 148 references it cites were found in a registry or an index.
The lipocalin protein family: structure and function
Open accessAbstract
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.
Overview
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
Cites
Statistics
Verification
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?
In the citing paper
“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.
Citations
Cites
Comprehensive insect physiology, biochemistry and pharmacology
Brooks, G. T. (1985) · Insect Biochemistry · doi:10.1016/0020-1790(85)90131-3 · Cited by 1,595
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
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
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
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
McSweeney, P. L. H., & Fox, P. F. (2013) · Springer eBooks · doi:10.1007/978-1-4614-4714-6 · Cited by 502
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 413
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
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
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
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
Cited by
Sorted by citations
Items 601–700 of 1,001
Crystal structure of MTCP-1: Implications for role of TCL-1 and MTCP-1 in T cell malignancies
Fu, Z., Bois, G. C. D., Song, S. P., Kulikovskaya, I. M., Virgilio, L., Rothstein, J. L., Croce, C. M., Weber, I. T., & Harrison, R. W. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3413 · Cited by 35
Update on optimized purification and characterization of natural milk allergens
Blanc, F., Bernard, H., Alessandri, S., Bublin, M., Paty, E., Leung, S. A., Adel‐Patient, K., & Wal, J. M. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700283 · Cited by 34
Lipocalin 2 Antagonizes the Proangiogenic Action of Ras in Transformed Cells
Venkatesha, S., Hanai, J., Seth, P., Karumanchi, S. A., & Sukhatme, V. P. (2006) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-06-0110 · Cited by 34
Evoli, S., Guzzi, R., & Rizzuti, B. (2014) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24625 · Cited by 34
The potential of component-resolved diagnosis in laboratory diagnostics of allergy
Dodig, S., & Čepelak, I. (2018) · Biochemia Medica · doi:10.11613/bm.2018.020501 · Cited by 35
Mans, B. J. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00530 · Cited by 34
Miyamoto, Y., Nishimura, S., Inoue, K., Shimamoto, S., Yoshida, T., Fukuhara, A., Yamada, M., Urade, Y., Yagi, N., Ohkubo, T., et al. (2009) · Journal of Structural Biology · doi:10.1016/j.jsb.2009.10.005 · Cited by 34
Intrinsic properties of allergens and environmental exposure as determinants of allergenicity*
Pomés, A. (2002) · Allergy · doi:10.1034/j.1398-9995.2002.02160.x · Cited by 34
Crystal structure of the human odorant binding protein, OBPIIa
Schiefner, A., Freier, R., Eichinger, A., & Skerra, A. (2015) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24797 · Cited by 34
Oakley, A. J., Bhatia, S., Ecroyd, H. W., & Garner, B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034057 · Cited by 34
Giasson, J., Li, G. H., & Chen, Y. (2011) · Inflammation & Allergy - Drug Targets · doi:10.2174/187152811796117753 · Cited by 34
Piotte, C. P., Hunter, A. K., Marshall, C. J., & Grigor, M. R. (1998) · Journal of Molecular Evolution · doi:10.1007/pl00006313 · Cited by 34
Charneau, S. O., Junqueira, M., Costa, C. M., Pires, D. L., Fernandes, E. S., Bussacos, A., de Sousa, M. V., Ricart, C. A. O., Shevchenko, A., & Teixeira, A. R. L. (2007) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2007.05.004 · Cited by 34
Fouchécourt, S., Lareyre, J., Chaurand, P., DaGue, B. B., Suzuki, K., Ong, D. E., Olson, G. E., Matusik, R. J., Caprioli, R. M., & Orgebin‐Crist, M. (2003) · Endocrinology · doi:10.1210/en.2002-220932 · Cited by 34
Role of Adipokines in Sarcopenia
Lu, W., Feng, W., Lai, J., Yuan, D., Xiao, W., & Li, Y. (2023) · Chinese Medical Journal · doi:10.1097/cm9.0000000000002255 · Cited by 34
Buemi, A., Musuamba, F. T., Stephan, F., Douhet, A., Meyer, M. D., Pauw, L. D., Darius, T., Kanaan, N., Wallemacq, P. E., & Mourad, M. (2014) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2014.06.079 · Cited by 33
Wu, B., Li, C., Du, Z., Yao, Q., Wu, J., Li, F., Zhang, P., Li, S., Xu, L., & Li, E. (2014) · Scientific Reports · doi:10.1038/srep05403 · Cited by 33
Adipose proteome analysis: focus on mediators of insulin resistance
Chen, X., & Hess, S. Y. (2008) · Expert Review of Proteomics · doi:10.1586/14789450.5.6.827 · Cited by 33
A novel mutation in LMBRD1 causes the cblF defect of vitamin B 12 metabolism in a Turkish patient
Gailus, S., Suormala, T., Malerczyk‐Aktas, A. G., Toliat, M. R., Wittkampf, T., Stucki, M., Nürnberg, P., Fowler, B., Hennermann, J. B., & Rutsch, F. (2010) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-009-9032-7 · Cited by 33
Pomés, A., Chruszcz, M., Gustchina, A., Minor, W., Mueller, G. A., Pedersen, L. C., Wlodawer, A., & Chapman, M. D. (2015) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2015.05.016 · Cited by 33
An, S., Zang, X., Yuan, W., Zhuge, Y., & Yu, Q. (2012) · Renal Failure · doi:10.3109/0886022x.2012.741877 · Cited by 33
Jin, Z. H., Kim, K. E., Shin, H. J., Jeong, E. A., Park, K.-A., Lee, J. Y., An, H. S., Choi, E. B., Jeong, J. H., Kwak, W., et al. (2020) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlaa017 · Cited by 34
Burda, P., Crosskey, T., Lauk, K., Zurborg, A., Söhnchen, C., Liffner, B., Wilcke, L., Pietsch, E. C., Strauss, J., Jeffries, C. M., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107817 · Cited by 33
Regulation of Sexually Dimorphic Expression of Major Urinary Proteins
Penn, D. J., Zala, S. M., & Luzynski, K. C. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.822073 · Cited by 36
Vinaiphat, A., Pazhanchamy, K., JebaMercy, G., Ngan, S. C., Leow, M. K., Ho, H. H., Gao, Y., Lim, K. L., Richards, M., de Kleijn, D. P. V., et al. (2023) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.122.318439 · Cited by 32
Interaction of Purified Tear Lipocalin with Lipid Membranes
̈, H. S.-S. ̈., Jauhiainen, M., Tervo, T., Redl, B., Kinnunen, P. K. J., & Holopainen, J. M. (2005) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.05-0176 · Cited by 33
Hippocampal apolipoprotein D level depends on Braak stage and APOE genotype
Glöckner, F., & Ohm, T. G. (2003) · Neuroscience · doi:10.1016/s0306-4522(03)00529-3 · Cited by 22
Hakk, H., Huwe, J. K., & Larsen, G. L. (2009) · Xenobiotica · doi:10.1080/00498250802546853 · Cited by 33
The major urinary protein system in the rat
Gómez‐Baena, G., Armstrong, S. D., Phelan, M. M., Hurst, J. L., & Beynon, R. J. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140083 · Cited by 33
Metabolism of 2,2′,4,4′-Tetrabromodiphenyl Ether (BDE-47) in Chickens
Hakk, H., Huwe, J. K., Murphy, K., & Rutherford, D. N. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf1012924 · Cited by 33
A systematic analysis of human lipocalin family and its expression in esophageal carcinoma
Du, Z., Wu, B., Wu, X., Lin, X., Qiu, X., Zhan, X.-F., Wang, S., Shen, J., Zheng, C.-P., Wu, Z., et al. (2015) · Scientific Reports · doi:10.1038/srep12010 · Cited by 34
Wille, H., Mandelkow�, E., & Mandelkow�, E. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50080-1 · Cited by 33
Berryhill, B. L., Beales, M. P., & Hassell, J. R. (2001) · PubMed · Cited by 33
Matsushita, F., Miyawaki, A., & Mikoshiba, K. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2104 · Cited by 33
Mouse Lipocalins (MUP, OBP, LCN) Are Co-expressed in Tissues Involved in Chemical Communication
Stopková, R., Vinkler, D., Kuntová, B., Šedo, O., Albrecht, T., Suchan, J., Komrsková, K., Zdráhal, Z., & Stopka, P. (2016) · Frontiers in Ecology and Evolution · doi:10.3389/fevo.2016.00047 · Cited by 32
Dcf1 Triggers Dendritic Spine Formation and Facilitates Memory Acquisition
Liu, Q., Feng, R., Chen, Y., Luo, G., Huang, Y. X., Chen, L., Lin, R., Ding, Y., & Wen, T. (2017) · Molecular Neurobiology · doi:10.1007/s12035-016-0349-6 · Cited by 32
Acute Phase Protein Levels as An Auxiliary Tool in Diagnosing Viral Diseases in Ruminants—A Review
Reczyńska, D., Zalewska, M., Czopowicz, M., Kaba, J., Zwierzchowski, L., & Bagnicka, E. (2018) · Viruses · doi:10.3390/v10090502 · Cited by 32
Gao, H., Ma, H., Sun, J., Xu, W., Gao, W., Lai, X., & Yan, B. (2021) · Journal of Experimental Zoology Part B Molecular and Developmental Evolution · doi:10.1002/jez.b.23025 · Cited by 32
Using lipocalin as a prognostic biomarker in acute kidney injury
Chen, J., Lee, T. H., Lee, C., & Chang, C. (2021) · Expert Review of Molecular Diagnostics · doi:10.1080/14737159.2021.1917384 · Cited by 32
Knipp, M., Zhang, H., Berry, R. E., & Walker, F. A. (2007) · Protein Expression and Purification · doi:10.1016/j.pep.2007.02.017 · Cited by 32
Ausili, A., Scirè, A., Damiani, E., Zolese, G., Bertoli, E., & Tanfani, F. (2005) · Biochemistry · doi:10.1021/bi051512z · Cited by 32
Ligand entry into the calyx of β‐lactoglobulin
Bello, M., & García‐Hernández, E. (2013) · Biopolymers · doi:10.1002/bip.22454 · Cited by 32
Wex, T., Lipyansky, A., Brömme, N. C., Wex, H., Guan, X. Q., & Brömme, D. (2001) · Biochemistry · doi:10.1021/bi002266o · Cited by 32
Trott, J. F., Wilson, M. J., Hovey, R. C., Shaw, D. C., & Nicholas, K. R. (2002) · Gene · doi:10.1016/s0378-1119(01)00883-6 · Cited by 32
Molecular and Crystal Properties of Bos d 2, an Allergenic Protein of the Lipocalin Family
Rautiainen, J. M., Auriola, S. O. K., Rouvinen, J., Kauppinen, J., Zeiler, T. A., Novikov, D., Virtanen, T. I., & MÄNTYJÄRVI, R. A. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8851 · Cited by 32
Redl, B., Merschak, P., Abt, B., & Wojnar, P. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01331-9 · Cited by 32
Wester, L., Johansson, M. U., & Åkerström, B. (1997) · Protein Expression and Purification · doi:10.1006/prep.1997.0760 · Cited by 32
Cornette, R., Farine, J., Abed-Vieillard, D., Quennedey, B., & Brossut, R. (2003) · Biochemical Journal · doi:10.1042/bj20030025 · Cited by 32
Hendricks, J. C. (2003) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00904.2002 · Cited by 32
Walker, F. A., & Simonis, U. (2005) · Encyclopedia of Inorganic Chemistry · doi:10.1002/0470862106.ia111 · Cited by 32
Apolipoprotein D Internalization Is a Basigin-dependent Mechanism
Najyb, O., Brissette, L., & Rassart, É. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.644302 · Cited by 32
Jeong, E. A., Lee, J., Shin, H. J., Lee, J. Y., Kim, K. E., An, H. S., Kim, D. R., Choi, K. Y., Lee, K. H., & Roh, G. S. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02331-8 · Cited by 31
Nitric oxide boosts TLR‐4 mediated lipocalin 2 expression in chondrocytes
Gómez, R., Scotece, M., Conde, J., López, V. A. M., Pino, J., Lago, F., Gómez-Reino, J. J., & Gualillo, O. (2013) · Journal of Orthopaedic Research® · doi:10.1002/jor.22331 · Cited by 32
Hakk, H., Diliberto, J. J., & Birnbaum, L. S. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.08.009 · Cited by 31
Knockdown of FIBRILLIN4 Gene Expression in Apple Decreases Plastoglobule Plastoquinone Content
Singh, D. K., Laremore, T. N., Smith, P. B. W., Maximova, S. N., & McNellis, T. W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047547 · Cited by 31
Apoptosis induced by uterine 24p3 protein in endometrial carcinoma cell line
Lin, H. H., Li, W., Lee, Y., & Chu, S.-T. (2007) · Toxicology · doi:10.1016/j.tox.2007.02.017 · Cited by 31
The Structure, Stability and Pheromone Binding of the Male Mouse Protein Sex Pheromone Darcin
Phelan, M. M., McLean, L., Armstrong, S. D., Hurst, J. L., Beynon, R. J., & Lian, L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0108415 · Cited by 31
Rhipicephalus (Boophilus) microplus
Pereira, M. D. C., & Labruna, M. B. (2008) · Cited by 31
Protein domain of chicken α1-acid glycoprotein is responsible for chiral recognition
Sadakane, Y., Matsunaga, H., Nakagomi, K., Hatanaka, Y., & Haginaka, J. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00716-7 · Cited by 31
Hoo, R. L. C., Yeung, D. C. Y., Lam, K. S., & Xu, A. (2007) · Expert Review of Endocrinology & Metabolism · doi:10.1586/17446651.3.1.29 · Cited by 31
Novel frameworks as a source of high-affinity ligands
Ladner, R. C., & Ley, A. C. (2001) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(00)00235-4 · Cited by 31
Glycodelin: a reproduction-related lipocalin
Halttunen, M., Kämäräinen, M., & Koistinen, H. K. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00158-8 · Cited by 31
Antipsychotic drugs differentially modulate apolipoprotein D in rat brain
Khan, M. M., Parikh, V., & Mahadik, S. P. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01866.x · Cited by 31
KAUPPINEN, ZEILER, Rautiainen, Rytkönen-Nissinen, M. A., TAIVAINEN, MÄNTYJÄRVI, & Virtanen (1999) · Clinical & Experimental Allergy · doi:10.1046/j.1365-2222.1999.00605.x · Cited by 31
Origin and Evolution of the Major Constituents of Milk
Oftedal, O. T. (2012) · Springer eBooks · doi:10.1007/978-1-4614-4714-6_1 · Cited by 31
Bensaoud, C., Aounallah, H., Sciani, J. M., Faria, F., Chudzinski‐Tavassi, A. M., Bouattour, A., & M’ghirbi, Y. (2019) · BMC Genomics · doi:10.1186/s12864-019-6042-1 · Cited by 30
Li, C., He, M., Yun, Y., & Peng, Y. (2019) · Journal of Invertebrate Pathology · doi:10.1016/j.jip.2019.107307 · Cited by 30
Astroglial and oligodendroglial markers in the cuprizone animal model for de- and remyelination
Castillo-Rodriguez, M. D. L. A., Gingele, S., Schröder, L., Möllenkamp, T. M., Stangel, M., Skripuletz, T., & Gudi, V. (2022) · Histochemistry and Cell Biology · doi:10.1007/s00418-022-02096-y · Cited by 33
Limanjaya, A., Yin, G. N., Hong, S., Kang, J., Gho, Y. S., Suh, J., & Ryu, J. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.72243 · Cited by 30
Determination of the T cell epitopes of the lipocalin allergen, Rat n 1
Jeal, H., Draper, A., Harris, J. M., Taylor, A. J. N., Cullinan, P., & Jones, M. G. K. (2004) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2004.02126.x · Cited by 30
Amniotic fluid elicits appetitive responses in human newborns: fatty acids and appetitive responses.
Contreras, C. M., Gutiérrez-García, A. G., Mendoza-López, R., Rodríguez-Landa, J., Bernal-Morales, B., & Díaz-Marte, C. (2013) · Developmental Psychobiology · doi:10.1002/dev.21012 · Cited by 32
Rodriguez-Valle, M., Moolhuijzen, P., Piper, E. K., Weiss, O., Vance, M. E., Bellgard, M., & Tabor, A. E. (2013) · International Journal for Parasitology · doi:10.1016/j.ijpara.2013.04.005 · Cited by 30
Conjugation of functional oligosaccharides reduced in vitro allergenicity of β-lactoglobulin
Wu, X., Liu, M., Xia, L., Wu, H., Liu, Z., & Xu, X. (2012) · Food and Agricultural Immunology · doi:10.1080/09540105.2012.686990 · Cited by 30
Functional Changes in β-Lactoglobulin upon Conjugation with Carboxymethyl Cyclodextrin
Hattori, M., Okada, Y., & Takahashi, K. (2000) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf000204z · Cited by 30
Huang, J. X., Cooper, M. A., Baker, M. A., Azad, M. A. K., Nation, R. L., Li, J., & Velkov, T. (2012) · Journal of Molecular Recognition · doi:10.1002/jmr.2221 · Cited by 30
Qiao, F., Luo, L., Peng, H., Luo, S., Huang, W., Cui, J., Li, X., Kong, L., Jiāng, D., Chitwood, D. J., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0160003 · Cited by 30
Altered mitochondrial and peroxisomal integrity in lipocalin-2-deficient mice with hepatic steatosis
Asimakopoulou, A., Fülöp, A., Borkham‐Kamphorst, E., de Leur, E. V., Gaßler, N., Berger, T., Beine, B., Meyer, H. E., Mak, T. W., Hopf, C., et al. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.04.006 · Cited by 30
Obesity-promoting and anti-thermogenic effects of neutrophil gelatinase-associated lipocalin in mice
Ishii, A., Katsuura, G., Imamaki, H., Kimura, H., Mori, K. P., Kuwabara, T., Kasahara, M., Yokoi, H., Ohinata, K., Kawanishi, T., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-15825-4 · Cited by 30
Kerstens, S., Murray, B. S., & Dickinson, E. (2004) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2004.10.026 · Cited by 30
Wen, C., Smith, R., & Banks, J. A. (1999) · The Plant Cell · doi:10.1105/tpc.11.7.1307 · Cited by 30
Jin, Y., & Manabe, T. (2005) · Electrophoresis · doi:10.1002/elps.200410187 · Cited by 30
Parisi, M., Mazzini, A., Sorbi, R. T., Ramoni, R., Grolli, S., & Favilla, R. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.08.009 · Cited by 30
Hiseni, A., Otten, L. G., & Arends, I. W. C. E. (2015) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-015-6998-y · Cited by 29
Nanobodys: Strategien zur chemischen Funktionalisierung und intrazelluläre Anwendungen
Schumacher, D., Helma, J., Schneider, A. F. L., Leonhardt, H., & Hackenberger, C. P. R. (2017) · Angewandte Chemie · doi:10.1002/ange.201708459 · Cited by 29
Bensaoud, C., Nishiyama, M. Y., Hamda, C. B., Lichtenstein, F., de Oliveira, Ú. C., Faria, F., Junqueira-de-Azevedo, I. L. M., Ghedira, K., Bouattour, A., M’ghirbi, Y., et al. (2018) · Parasites & Vectors · doi:10.1186/s13071-018-2874-9 · Cited by 29
Yaguchi, H., Shigenobu, S., Hayashi, Y., Miyazaki, S., Toga, K., Masuoka, Y., & Maekawa, K. (2018) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.2018.0707 · Cited by 29
Varlamova, E. G., & Zaripov, O. G. (2020) · Research in Veterinary Science · doi:10.1016/j.rvsc.2020.08.014 · Cited by 29
Santoro, D. D. F., de Sousa, L. B., Câmara, N. O. S., de Freitas, D., & de Oliveira, L. A. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.612319 · Cited by 29
Harterink, M., & Korswagen, H. C. (2011) · Acta Physiologica · doi:10.1111/j.1748-1716.2011.02287.x · Cited by 29
pH-Dependent Conformational Changes in Tear Lipocalin by Site-Directed Tryptophan Fluorescence
Gasymov, O. K., Abduragimov, A. R., & Glasgow, B. J. (2009) · Biochemistry · doi:10.1021/bi901435q · Cited by 29
Tong, Z., Chakraborty, S., Sung, B., Koolwal, P., Kaur, S., Aggarwal, B. B., Mani, S. A., Bresalier, R. S., Batra, S. K., & Guha, S. (2010) · Cancer · doi:10.1002/cncr.25803 · Cited by 29
Sickinger, S., Maier, H. T., König, S., Vallant, N., Kofler, M., Schumpp, P., Schwelberger, H. G., Hermann, M., Obrist, P., Schneeberger, S., et al. (2013) · Transplant International · doi:10.1111/tri.12116 · Cited by 29
Mechanistic events underlying odorant binding protein chemoreception
Golebiowski, J., Antonczak, S., Fiorucci, S., & Cabrol‐Bass, D. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21307 · Cited by 29
Uehara, H., Takahashi, T., & Izumi, K. (2013) · International Journal of Oncology · doi:10.3892/ijo.2013.1954 · Cited by 28
Wang, Y., Li, Z., Zhou, Y., Cao, J., Zhang, H., Gong, H., & Zhou, J. (2016) · Parasites & Vectors · doi:10.1186/s13071-016-1790-0 · Cited by 29
Dissociation and unfolding of bovine odorant binding protein at acidic pH
Mazzini, A., Polverini, E., Parisi, M., Sorbi, R. T., & Favilla, R. (2007) · Journal of Structural Biology · doi:10.1016/j.jsb.2007.02.007 · Cited by 29
Rational engineering of a fluorescein-binding anticalin for improved ligand affinity
Vopel, S., Mohr, H., & Skerra, A. (2005) · Biological Chemistry · doi:10.1515/bc.2005.126 · Cited by 29
Binding free energy prediction in strongly hydrophobic biomolecular systems
Charlier, L., Nespoulous, C., Fiorucci, S., Antonczak, S., & Golebiowski, J. (2007) · Physical Chemistry Chemical Physics · doi:10.1039/b710186d · Cited by 29
Baer, C., Retief, J., Niel, E. E. V., Braiman, M. S., & Gonzalez-Fernandez, F. (1998) · Experimental Eye Research · doi:10.1006/exer.1997.0418 · Cited by 29
Yanagisawa, R., Takano, H., Inoue, K., Ichinose, T., Yoshida, S., Sadakane, K., Takeda, K., Yoshino, S., Yamaki, K., Kumagai, Y., et al. (2004) · Experimental Biology and Medicine · doi:10.1177/153537020422901013 · Cited by 29
Metadata
- 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
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › 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
