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 301–400 of 867
Anticalin® proteins: from bench to bedside
Deuschle, F., Ilyukhina, E., & Skerra, A. (2020) · Expert Opinion on Biological Therapy · doi:10.1080/14712598.2021.1839046 · Cited by 35
Biosensor array based on ligand binding proteins for narcotics and explosives detection
Scorsone, E., Manai, R., Cali, K., Ricatti, M. J., Farno, S., Persaud, K. C., & Mucignat‐Caretta, C. (2021) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2021.129587 · Cited by 35
Valkenburgh, J. S. V., Meuret, C. J., Martinez, A. E., Kodancha, V., Solomon, V. A., Chen, K., & Yassine, H. N. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.700847 · Cited by 38
Apolipoprotein M: Research progress, regulation and metabolic functions (Review)
Huang, L., Gao, J., Pu, C., Zhang, P. J., Wang, L., Feng, G. L., & Zhang, Y. (2015) · Molecular Medicine Reports · doi:10.3892/mmr.2015.3658 · Cited by 34
An Insight Into the Sialotranscriptome of Triatoma rubida (Hemiptera: Heteroptera)
Ribeiro, J. M. C., Assumpção, T. C. F., Pham, M., Francischetti, I. M. B., & Reisenman, C. E. (2012) · Journal of Medical Entomology · doi:10.1603/me11243 · Cited by 34
Are recently reported biomarkers helpful for early and accurate diagnosis of acute kidney injury?
Barrera‐Chimal, J., & Bobadilla, N. A. (2012) · Biomarkers · doi:10.3109/1354750x.2012.680070 · Cited by 34
Meyers, K. R., López, M., Ho, J., Wills, S., Rayalam, S., & Taval, S. (2020) · Scientific Reports · doi:10.1038/s41598-020-71249-7 · 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
Molecular mechanism of enzymatic allene oxide cyclization in plants
Hofmann, E., & Pollmann, S. (2008) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2007.12.007 · Cited by 35
Xu, N., Nilsson‐Ehle, P., & Åhrén, B. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.02.022 · Cited by 34
Importance of fatty acid binding proteins in cellular function and organismal metabolism
Agellon, L. B. (2023) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17703 · Cited by 33
Ji, L., Zhang, Z., Liu, S., Liyan, Z., Li, Q., Xiao, B., Suzuki, N., Burks, D. J., Azad, R. K., & Xie, G. (2023) · The Plant Journal · doi:10.1111/tpj.16470 · Cited by 33
Kronfel, C. M., Kuzin, A. P., Forouhar, F., Biswas, A., Su, M., Lew, S., Seetharaman, J., Xiao, R., Everett, J. K., Ma, L.-C., et al. (2013) · Biochemistry · doi:10.1021/bi401192z · Cited by 33
The role of lipocalins in airway disease
Dittrich, A., Meyer, H., & Hamelmann, E. H. (2012) · Clinical & Experimental Allergy · doi:10.1111/cea.12025 · Cited by 33
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
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
THz absorption spectroscopy of solvated β-lactoglobulin
Vondracek, H., Dielmann-Gessner, J., Lubitz, W., Knipp, M., & Havenith, M. (2014) · The Journal of Chemical Physics · doi:10.1063/1.4903237 · Cited by 32
Portman, K. L., Long, J., Carr, S. B., Briand, L. V., Winzor, D. J., Searle, M. S., & Scott, D. J. (2014) · Biochemistry · doi:10.1021/bi5002344 · Cited by 32
Gustatory Mechanisms for Fat Detection
Gilbertson, T. A., Yu, T., & Shah, B. P. (2009) · Frontiers in neuroscience · doi:10.1201/9781420067767-c3 · Cited by 34
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
From radioactive ligands to biosensors: binding methods with olfactory proteins
Pelosi, P., Zhu, J., & Knoll, W. (2018) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-018-9253-5 · Cited by 32
Törüner, F. B., Altınova, A. E., Aktürk, M., Kaya, M., Arslan, E., Bukan, N. C., Kan, E., Yetkin, İ., & Arslan, M. (2010) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2010.11.011 · Cited by 32
Human α-1-Microglobulin Is Covalently Bound to Kynurenine-derived Chromophores
Sala, A., Campagnoli, M., Perani, E., Romano, A., Labò, S., Monzani, E., Minchiotti, L., & Galliano, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408242200 · Cited by 32
Miyamoto, T., Kashima, H., 鈴木, 昭., Kikuchi, N., Konishi, I., Seki, N., & Shiozawa, T. (2011) · Human Pathology · doi:10.1016/j.humpath.2010.07.027 · Cited by 32
Lipocalin-7 Is a Matricellular Regulator of Angiogenesis
Brown, L. J., Alawoki, M., Crawford, M. E., Reida, T., Sears, A., Torma, T., & Albig, A. R. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013905 · Cited by 32
Ureteric bud controls multiple steps in the conversion of mesenchyme to epithelia
Mori, K., Yang, J., & Barasch, J. M. (2003) · Seminars in Cell and Developmental Biology · doi:10.1016/s1084-9521(03)00023-5 · Cited by 32
Hendricks, J. C. (2003) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00904.2002 · Cited by 32
Mazzini, A., Maia, A., Parisi, M., Sorbi, R. T., Ramoni, R., Grolli, S., & Favilla, R. (2002) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/s1570-9639(02)00404-1 · Cited by 31
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
An Impedimetric Biosensor for Detection of Volatile Organic Compounds in Food
Calabrese, A., Battistoni, P., Ceylan, S., Zeni, L., Capo, A., Varriale, A., D’Auria, S., & Staiano, M. (2023) · Biosensors · doi:10.3390/bios13030341 · 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
Porez, G., Gross, B. S., Prawitt, J., Gheeraert, C., Berrabah, W., Alexandre, J., Staels, B., & Lefèbvre, P. (2013) · Endocrinology · doi:10.1210/en.2013-1263 · Cited by 34
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
Fujimori, K., Kadoyama, K., & Urade, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411755200 · Cited by 38
Beyond sequence: Structure-based machine learning
Durairaj, J., de Ridder, D., & van Dijk, A. D. J. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.12.039 · Cited by 32
Ebrahimi, M., Roudkenar, M. H., Fooladi, A. A. I., Halabian, R., Ghanei, M., Kondo, H., & Nourani, M. R. (2010) · BioMed Research International · doi:10.1155/2010/823131 · Cited by 30
Melis, M., Sollai, G., Masala, C., Pisanu, C., Cossu, G., Melis, M., Sarchioto, M., Oppo, V., Morelli, M., Crnjar, R., et al. (2019) · Chemical Senses · doi:10.1093/chemse/bjz020 · Cited by 30
Chien, M., Ying, T.-H., Yang, S., Yu, J.-K., Hsu, C.-W., Hsieh, S.-C., & Hsieh, Y. (2012) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-012-9370-1 · Cited by 30
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
Sade, D., Eybishtz, A., Gorovits, R., Sobol, I., & Czosnek, H. H. (2012) · Plant Molecular Biology · doi:10.1007/s11103-012-9946-6 · Cited by 30
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
Khan, K. N. M., Hard, G. C., & Alden, C. L. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-415759-0.00047-9 · Cited by 31
Yongliang Fan, A., Gore, J. C., Redding, K. O., Vailes, L. D., Chapman, M. D., & Schal, C. (2005) · Insect Molecular Biology · doi:10.1111/j.1365-2583.2004.00530.x · Cited by 30
Zsila, F., Imre, T., Szabó, P. T., Bikádi, Z., & Simonyi, M. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02771-0 · Cited by 29
Lipocalin-2 Alleviates LPS-Induced Inflammation Through Alteration of Macrophage Properties
Du, H., Li, L., Li, J. H., Xiong, Q., Yu, X., & Yu, H. B. (2021) · Journal of Inflammation Research · doi:10.2147/jir.s328916 · Cited by 29
The major horse allergen Equ c 1 contains one immunodominant region of T cell epitopes
Immonen, A. K., Kinnunen, T. T., Sirven, P., Taivainen, A. H., Houitte, D., Peräsaari, J. P., Närvänen, A. T. O., Saarelainen, S. A., Rytkönen-Nissinen, M. A., Maillère, B., et al. (2007) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2007.02722.x · Cited by 29
Mohammadi, F., Sahihi, M., & Bordbar, A. (2015) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2014.12.032 · Cited by 29
Lipocalin 13 regulation of glucose and lipid metabolism in obesity
Zhou, Y., & Rui, L. (2013) · Vitamins & Hormones · doi:10.1016/b978-0-12-407766-9.00015-8 · Cited by 28
Bianchi, F., Flisi, S., Careri, M., Riboni, N., Resimini, S., Sala, A., Conti, V., Mattarozzi, M., Taddei, S., Spadini, C., et al. (2019) · PLoS ONE · doi:10.1371/journal.pone.0213545 · Cited by 28
Glia-based biomarkers and their functional role in the CNS
Jha, M. K., & Suk, K. (2013) · Expert Review of Proteomics · doi:10.1586/epr.12.70 · Cited by 28
Nies, D. H., & Grass, G. (2009) · EcoSal Plus · doi:10.1128/ecosalplus.5.4.4.3 · Cited by 31
Kume, S., Lee, Y., Miyamoto, Y., Fukada, H., Goto, Y., & Inui, T. (2012) · Biochemical Journal · doi:10.1042/bj20120324 · Cited by 28
Progress in the Pathogenesis of Diabetic Encephalopathy: The Key Role of Neuroinflammation
Luo, Y., Zhu, J., Hu, Z., Luo, W., Du, X., Hu, H., & Peng, S. (2024) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.3841 · Cited by 29
Biochemical basis for activation of virulence genes by bile salts inVibrio parahaemolyticus
Rivera‐Cancel, G., & Orth, K. (2017) · Gut Microbes · doi:10.1080/19490976.2017.1287655 · Cited by 27
Characterization and Primary Functional Analysis of a Bamboo ZEP Gene from Phyllostachys edulis
Lou, Y., Sun, H., Li, L., Zhao, H., & Gao, Z. (2017) · DNA and Cell Biology · doi:10.1089/dna.2017.3705 · Cited by 27
Hernández-Gras, F., & Boronat, A. (2015) · Plant Molecular Biology · doi:10.1007/s11103-015-0326-x · Cited by 27
Adipose-Derived Lipid-Binding Proteins: The Good, the Bad and the Metabolic Diseases
Frances, L., Tavernier, G., & Viguerie, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910460 · Cited by 29
Identification of new altered genes in rat cochleae with noise-induced hearing loss
Han, Y., Hong, L., Zhong, C., Chen, Y., Wang, Y., Mao, X., Zhao, D., & Qiu, J. (2012) · Gene · doi:10.1016/j.gene.2012.02.042 · Cited by 27
Wu, Y., Kim, J. Y., Zhou, S., & Smas, C. M. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-397 · Cited by 27
Exogenous Lipocalin 2 Ameliorates Acute Rejection in a Mouse Model of Renal Transplantation
Ashraf, M., Schwelberger, H. G., Brendel, K., Feurle, J., Andrassy, J., Kotsch, K., Regele, H. M., Pratschke, J., Maier, H. T., & Aigner, F. (2015) · American Journal of Transplantation · doi:10.1111/ajt.13521 · Cited by 28
Yamamoto, K., Ishibashi, O., Sugiura, K., Ubatani, M., Sakaguchi, M., Nakatsuji, M., Shimamoto, S., Noda, M., Uchiyama, S., Fukutomi, Y., et al. (2019) · Scientific Reports · doi:10.1038/s41598-018-38134-w · Cited by 27
Wojnar, P., Dirnhofer, S., Ladurner, P., Berger, P., & Redl, B. (2002) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215540205000314 · Cited by 27
Peres, L. A. B., Júnior, A. D. D. C., Assumpção, R. A. B., 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. (2014) · Brazilian Journal of Nephrology · doi:10.5935/0101-2800.20140041 · Cited by 26
The v-myc-induced Q83 Lipocalin Is a Siderocalin
Coudevylle, N., Geist, L., Hötzinger, M., Hartl, M., Kontaxis, G., Bister, K., & Konrat, R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.123331 · Cited by 26
Mans, B. J., & Neitz, A. W. H. (2004) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2004.03.006 · Cited by 26
Antennal Protein Profile in Honeybees: Caste and Task Matter More Than Age
Iovinella, I., Cappa, F., Cini, A., Petrocelli, I., Cervo, R., Turillazzi, S., & Dani, F. R. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00748 · Cited by 26
Luthra, A., Montezuma-Rusca, J. M., Vake, C. J. L., LeDoyt, M., Delgado, K. N., Davenport, T. C., Fiel-Gan, M. D., Caimano, M. J., Radolf, J. D., & Hawley, K. L. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008871 · Cited by 25
Yang, G., Attardo, G. M., Lohs, C., & Aksoy, S. (2010) · Insect Molecular Biology · doi:10.1111/j.1365-2583.2009.00987.x · Cited by 26
Zsila, F. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00203-5 · Cited by 26
Ruiz, M., Wicker, C., Sánchez, D., & Ganfornina, M. D. (2012) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2012.07.005 · Cited by 29
Epididymis-specific lipocalin promoters
Suzuki, K., Yu, X., Chaurand, P., Araki, Y., Lareyre, J., Caprioli, R. M., Orgebin‐Crist, M., & Matusik, R. J. (2007) · Asian Journal of Andrology · doi:10.1111/j.1745-7262.2007.00300.x · Cited by 26
Compact Packing of Lipocalin-type Prostaglandin D Synthase Induced by Binding of Lipophilic Ligands
Inoue, K., Yagi, N., Urade, Y., & Inui, T. (2008) · The Journal of Biochemistry · doi:10.1093/jb/mvn154 · Cited by 26
He, C., Howes, B. D., Smulevich, G., Rumpel, S., Reijerse, E. J., Lubitz, W., Cox, N. J., & Knipp, M. (2015) · Journal of the American Chemical Society · doi:10.1021/ja512938u · Cited by 25
Ruby, M. A., Nomura, D. K., Hudak, C. S. S., Barber, A., Casida, J. E., & Krauss, R. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026415 · Cited by 26
Chen, X., Qiu, F. X., Zhao, X., Lu, J., Tan, X.-H., Xu, J., Chen, C., Zhang, F., Liu, C., Qiao, D., et al. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00559 · Cited by 24
Molecular Basis for Two Stereoselective Diels–Alderases that Produce Decalin Skeletons**
Fujiyama, K., Kato, N., Re, S., Kinugasa, K., Watanabe, K., Takita, R., Nogawa, T., Hino, T., Osada, H., Sugita, Y., et al. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202106186 · Cited by 25
Watanabe, K., Sato, M., & Osada, H. (2022) · Fungal Biology and Biotechnology · doi:10.1186/s40694-022-00139-6 · Cited by 27
Iron metabolism and regulation by neutrophil gelatinase-associated lipocalin in cardiomyopathy
Chan, Y. K., Sung, H. K., & Sweeney, G. (2015) · Clinical Science · doi:10.1042/cs20150075 · Cited by 27
Costa, D., Principi, E., Lazzarini, E., Descalzi, F., Cancedda, R., Castagnola, P., & Tavella, S. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25755 · Cited by 25
Lipocalin‐2: Its perspectives in brain pathology and possible roles in cognition
Pinyopornpanish, K., Chattipakorn, N., & Chattipakorn, S. C. (2019) · Journal of Neuroendocrinology · doi:10.1111/jne.12779 · Cited by 25
Maximizing lipocalin prediction through balanced and diversified training set and decision fusion
Nath, A., & Subbiah, K. (2015) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2015.09.011 · Cited by 25
Stepanenko, O. V., Stepanenko, O. V., Staiano, M., Kuznetsova, I. М., Константинович, Т. К., & D’Auria, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085169 · Cited by 24
Naguib, M. M., Feldman, N., Zarodkiewicz, P., Shropshire, H., Biamis, C., El-Halfawy, O. M., McCain, J., Dezanet, C., Décout, J., Chen, Y., et al. (2022) · PLoS Biology · doi:10.1371/journal.pbio.3001610 · Cited by 24
Fuchs, T., & Hewitt, P. G. (2011) · Biomarkers in Medicine · doi:10.2217/bmm.11.86 · Cited by 24
Wang, H.-H., Wu, M., Chan, M. W. Y., Pu, Y., Chen, C., & Lee, T. (2014) · Archives of Toxicology · doi:10.1007/s00204-014-1214-x · Cited by 24
Vetter, S. W., Terentis, A. C., Osborne, R. L., Dawson, J. H., & Goodin, D. B. (2008) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-008-0436-x · Cited by 24
Perez‐Miller, S., Zou, Q., Novotný, M. V., & Hurley, T. D. (2010) · Protein Science · doi:10.1002/pro.426 · Cited by 24
Biliverdin is the endogenous ligand of human serum α1-acid glycoprotein
Zsila, F., & Mády, G. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.05.090 · Cited by 24
Tear lipocalin: potential for selective delivery of rifampin
Gasymov, O. K., Abduragimov, A. R., Gasimov, E. O., Yusifov, T., Dooley, A. N., & Glasgow, B. J. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2003.11.006 · Cited by 24
Gonzalez-Fernandez, F., Baer, C. A., & Ghosh, D. (2007) · BMC Biochemistry · doi:10.1186/1471-2091-8-15 · Cited by 23
Huang, D., Jiao, X., Huang, S., Liu, J., Si, H., Qi, D., Pei, X., Lu, D., Wang, Y., & Li, Z. (2024) · The Ocular Surface · doi:10.1016/j.jtos.2024.06.005 · Cited by 23
Nardiello, M., Scieuzo, C., Salvia, R., Farina, D., Franco, A., Cammack, J. A., Tomberlin, J. K., Falabella, P., & Persaud, K. C. (2022) · Nanotechnology · doi:10.1088/1361-6528/ac51ab · Cited by 23
The mysterious role of fibrillin in plastid metabolism: current advances in understanding
Kim, I., & Kim, H. U. (2022) · Journal of Experimental Botany · doi:10.1093/jxb/erac087 · Cited by 23
Mans, B. J., Andersen, J. F., & Ribeiro, J. M. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415613 · Cited by 23
Wang, M., Zhu, X.-J., Yang, J., Dai, Z., Mahmood, K., Yang, F., & Yang, W. (2007) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2007.01.003 · Cited by 23
Attardo, G. M., Benoit, J. B., Michalková, V., Patrick, K. R., Krause, T. B., & Aksoy, S. (2014) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0002645 · Cited by 23
Jobichen, C., Fernandis, A. Z., Velázquez‐Campoy, A., Leung, K. Y., Mok, Y., Wenk, M. R., & Sivaraman, J. (2009) · Biochemical Journal · doi:10.1042/bj20081588 · Cited by 23
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