Lipocalins - a family portrait

The lipocalin protein family: structure and function

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

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

An Iron Delivery Pathway Mediated by a Lipocalin

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

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

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

The three‐dimensional structure of retinol‐binding protein.

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

The core lipocalin, bovine β-lactoglobulin

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

A Model for the Denaturation and Aggregation of β‐Lactoglobulin

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

Biochemistry of the violaxanthin cycle in higher plants

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

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

A Novel Human Apolipoprotein (apoM)

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

Molecular interactions of the neuronal GPI‐anchored lipocalin Lazarillo

Sánchez, D., Ortega‐Cubero, S., Åkerström, B., Herrera, M., Bastiani, M. J., & Ganfornina, M. D. (2008) · Journal of Molecular Recognition · doi:10.1002/jmr.902 · Cited by 16

Functional analyses of lipocalin proteins in tomato

Wahyudi, A., Ariyani, D., Ma, G., Inaba, R., Fukasawa, C., Nakano, R., & Motohashi, R. (2018) · Plant Biotechnology · doi:10.5511/plantbiotechnology.18.0620a · Cited by 16

Proteomic analysis of black poplar (Populus nigra L.) seed storability

Pawłowski, T. A., Klupczyńska, E. A., Staszak, A. M., & Suszka, J. (2019) · Annals of Forest Science · doi:10.1007/s13595-019-0887-y · Cited by 16

Cloning and functional study of lipocalin: retinol-binding protein-like gene family of the ridgetail white prawn, Exopalaemon carinicauda

Ma, H., Sun, J., Xu, W., Gao, W., Hu, G., Lai, X., Yan, B., & Gao, H. (2019) · Molecular Genetics and Genomics · doi:10.1007/s00438-019-01633-0 · Cited by 16

New transgenic line of Arabidopsis thaliana with partly disabled zeaxanthin epoxidase activity displays changed carotenoid composition, xanthophyll cycle activity and non-photochemical quenching kinetics

Nowicka, B., Strzałka, W., & Strzałka, K. (2009) · Journal of Plant Physiology · doi:10.1016/j.jplph.2008.12.010 · Cited by 15

Identification of functionally diverse lipocalin proteins from sequence information using support vector machine

Pugalenthi, G., Kandaswamy, K. K., Suganthan, P. N., Archunan, G., & Sowdhamini, R. (2010) · Amino Acids · doi:10.1007/s00726-010-0520-8 · Cited by 16

Investigating the interaction between the violaxanthin cycle enzyme zeaxanthin epoxidase and the thylakoid membrane

Schaller, S., Wilhelm, C., Strzałka, K., & Goss, R. (2012) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2012.05.019 · Cited by 15

A Novel Fatty Acid-Binding Protein-Like Carotenoid-Binding Protein from the Gonad of the New Zealand Sea Urchin Evechinus chloroticus

Brewster, J. L., Sabherwal, M., Garama, D. J., & Carne, A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0106465 · Cited by 15

Mutant bovine odorant‐binding protein: Temperature affects the protein stability and dynamics as revealed by infrared spectroscopy and molecular dynamics simulations

Marabotti, A., Lefèvre, T., Staiano, M., Crescenzo, R., Varriale, A., Rossi, M., Pézolet, M., & D’Auria, S. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21966 · Cited by 14

Hepatokines, bile acids and ketone bodies are novel Hormones regulating energy homeostasis

Garruti, G., Baj, J., Cignarelli, A., Perrini, S., & Giorgino, F. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1154561 · Cited by 15

Multiple Self‐Assembly Functional Structures Based on Versatile Binding Sites of β‐Lactoglobulin

Hendler, N., Belgorodsky, B., Mentovich, E., Richter, S. E., Fadeev, L., & Gozin, M. (2012) · Advanced Functional Materials · doi:10.1002/adfm.201102463 · Cited by 13

Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms

Stepanenko, O. V., Roginskii, D. O., Stepanenko, O. V., Kuznetsova, I. М., Uversky, V. N., & Константинович, Т. К. (2016) · PeerJ · doi:10.7717/peerj.1574 · Cited by 12

Serum Levels and Placental Expression of NGAL in Gestational Diabetes Mellitus

Yin, X., Huo, Y., Liu, L., Pan, Y., Liu, S., & Wang, R. (2020) · International Journal of Endocrinology · doi:10.1155/2020/8760563 · Cited by 12

Molecular basis for the interaction of cellular retinol binding protein 2 (CRBP2) with nonretinoid ligands

Silvaroli, J. A., Plau, J., Adams, C. H., Banerjee, S., Widjaja‐Adhi, M. A. K., Blaner, W. S., & Golczak, M. (2021) · Journal of Lipid Research · doi:10.1016/j.jlr.2021.100054 · Cited by 12

CRISPR/Cas9‐mediated disruption of lipocalins, Ly6g5b, and Ly6g5c causes male subfertility in mice

Sakurai, N., Fujihara, Y., Kobayashi, K., & Ikawa, M. (2022) · Andrology · doi:10.1111/andr.13350 · Cited by 12

The Harderian gland transcriptomes of Caraiba andreae, Cubophis cantherigerus and Tretanorhinus variabilis, three colubroid snakes from Cuba

Domínguez‐Pérez, D., Durbán, J., Agüero-Chapin, G., López, J. T., Molina, R., Almeida, D., Calvete, J. J., Vasconcelos, V. M., & Antunes, A. (2018) · Genomics · doi:10.1016/j.ygeno.2018.11.026 · Cited by 12

Modifications of the Carotenoid Metabolism in Plastids

Moulin, P., Lemoine, Y., & Schoefs, B. (2010) · Books in soils, plants, and the environment · doi:10.1201/b10329-20 · Cited by 12

Diversity of anti-haemostatic proteins in the salivary glands of Rhodnius species transmitters of Chagas disease in the greater Amazon

Bussacos, A., Nakayasu, E. S., Hecht, M. M., Parente, J. A., Soares, C. M. A., Teixeira, A. R. L., & de Almeida, I. C. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.06.022 · Cited by 11

Obstructor, a Frankliniella occidentalis protein, promotes transmission of tomato spotted wilt orthotospovirus

Zheng, X., Wan, Y., Tao, M., Yuan, J., Zhang, K., Wang, J., Zhang, Y., Liang, P., & Wu, Q. (2022) · Insect Science · doi:10.1111/1744-7917.13138 · Cited by 11

Occurrence of neoxanthin and lutein epoxide cycle in parasitic Cuscuta species.

Kruk, J., & Szymańska, R. (2008) · Acta Biochimica Polonica · doi:10.18388/abp.2008_3111 · Cited by 11

Structural Entities Associated with Different Lipid Phases of Plant Thylakoid Membranes—Selective Susceptibilities to Different Lipases and Proteases

Dlouhý, O., Karlický, V., Javornik, U., Kurasová, I., Zsíros, O., Šket, P., Kanna, S. D., Böde, K., Večeřová, K., Urban, O., et al. (2022) · Cells · doi:10.3390/cells11172681 · Cited by 10

Evolutionary and functional insights into Leishmania META1: evidence for lateral gene transfer and a role for META1 in secretion

Puri, V., Goyal, A., Sankaranarayanan, R., Enright, A. J., & Vaidya, T. B. (2011) · BMC Evolutionary Biology · doi:10.1186/1471-2148-11-334 · Cited by 10

Under Pressure That Splits a Family in Two. The Case of Lipocalin Family

Marchal, S., Marabotti, A., Staiano, M., Varriale, A., Domaschke, T., Lange, R., & D’Auria, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050489 · Cited by 9

An updated catalog of lipocalins of the chagas disease vector Rhodnius prolixus (Hemiptera, Reduviidae)

Santos, D. V., Gontijo, N. F., Pessoa, G. C. D., Sant'Anna, M. R. V., Araújo, R. N., Pereira, M. H., & Koerich, L. B. (2022) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2022.103797 · Cited by 9

Role of Small Molecule Ligands in IgE-Mediated Allergy

Khatri, K., O’Malley, A., Linn, C., Kowal, K., & Chruszcz, M. (2023) · Current Allergy and Asthma Reports · doi:10.1007/s11882-023-01100-2 · Cited by 9

Temperature‐induced lipocalin‐mediated membrane integrity: Possible implications for vindoline accumulation in Catharanthus roseus leaves

Mall, M., Shanker, K., Nagegowda, D. A., Samad, A., Kalra, A., Pandey, A., Sundaresan, V., & Shukla, A. K. (2023) · Physiologia Plantarum · doi:10.1111/ppl.13994 · Cited by 9

Overexpression of Wild Arachis Lipocalin Enhances Root-Knot Nematode Resistance in Peanut Hairy Roots

Pereira, B. M., Guimarães, L. A., Souza, N. O. S., Saraiva, M. A. P., Guimarães, P. M., & Brasileiro, A. C. M. (2019) · Plant Molecular Biology Reporter · doi:10.1007/s11105-019-01140-x · Cited by 9

Activation of six lipocalins genes’ transcription under PCB18 stress in OsTIL-silenced Oryza sativa L

Hao, D., Wang, H., & Niu, L. (2020) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2020.111063 · Cited by 9

Structural and ligand binding analysis of the pet allergens Can f 1 and Fel d 7

Min, J., Foo, A. C. Y., Gabel, S. A., Perera, L., DeRose, E. F., Pomés, A., Pedersen, L. C., & Mueller, G. A. (2023) · Frontiers in Allergy · doi:10.3389/falgy.2023.1133412 · Cited by 9

Conformational and biochemical characterization of a rat epididymis-specific lipocalin 12 expressed in Escherichia coli

Peng, Y., Liu, J., Liu, Q., Yao, Y.-H., Guo, C., Zhang, Y., & Lin, D. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.07.020 · Cited by 9

Cloning and primary characterizations of rLcn9, a new member of epididymal lipocalins in rat

Li, X., Zhan, X., Liu, S., Hu, S., Zhu, C., Hall, S. H., French, F. S., Liu, Q., & Zhang, Y. (2012) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gms072 · Cited by 9

Plasma lipocalin‐2 levels in pregnancy

CESUR, S., Yücel, A., Noyan, V., & Sağsöz, N. (2011) · Acta Obstetricia Et Gynecologica Scandinavica · doi:10.1111/j.1600-0412.2011.01158.x · Cited by 9

Tear Film Proteome of Healthy Domestic Cats

Veloso, J. F., Guedes, P. E. B., Lacerda, L. C., Santana, J. O., Mora-Ocampo, I. Y., Pirovani, C. P., Oriá, A. P., Munhoz, A. D., & Carlos, R. S. A. (2021) · Veterinary Medicine International · doi:10.1155/2021/8708023 · Cited by 8

Hepatokines and their role in cardiohepatic interactions in heart failure

Shouman, W. A., Najmeddine, S., Sinno, L., Nehme, R. D., Ghawi, A. E., Ziade, J. A., Altara, R., Amin, G., Booz, G. W., & Zouein, F. A. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.177356 · Cited by 9

NMR Structure of Lipoprotein YxeF from Bacillus subtilis Reveals a Calycin Fold and Distant Homology with the Lipocalin Blc from Escherichia coli

Wu, Y., Punta, M., Xiao, R., Acton, T., Sathyamoorthy, B., Dey, F., Fischer, M. J., Skerra, A., Rost, B., Montelione, G. T., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037404 · Cited by 8

DiB-splits: nature-guided design of a novel fluorescent labeling split system

Bozhanova, N. G., Gavrikov, A. S., Mishin, A. S., & Meiler, J. (2020) · Scientific Reports · doi:10.1038/s41598-020-67095-2 · Cited by 8

Model dependences of the deactivation of phytoplankton pigment excitation energy on environmental conditions in the sea**Support for this study was provided by the project ‘Satellite Monitoring of the Baltic Sea Environment - SatBałtyk’ funded by European Union through European Regional Development Fund contract No. POIG 01.01.02-22-011/09.

Ostrowska, M. (2012) · Oceanologia · doi:10.5697/oc.54-4.545 · Cited by 7

Expression and purification of cysteine mutation isoforms of rat lipocalin-type prostaglandin D synthase for nuclear magnetic resonance study

Liu, J., Lin, K., Guo, C., Gao, H., Yao, Y.-H., & Lin, D. (2008) · Acta Biochimica et Biophysica Sinica · doi:10.1111/j.1745-7270.2008.00426.x · Cited by 7

Ligand-Binding Proteins: Structure, Stability and Practical Application

Stepanenko, O. V., Fonin, A. V., Stepanenko, O. V., Kuznetsova, I. М., & Константинович, Т. К. (2012) · InTech eBooks · doi:10.5772/38013 · Cited by 6

An Experimental Approach for the Identification of Conserved Secreted Proteins in Trypanosomatids

Corrales, R. M., Mathieu-Daudé, F., Garcia, D., Brénière, S. F., & Séréno, D. (2010) · BioMed Research International · doi:10.1155/2010/752698 · Cited by 6

Wound Healing Effects of a Lipocalin-Derived Peptide

Tavassi, A. M. C. (2014) · Journal of Clinical Toxicology · doi:10.4172/2161-0495.1000187 · Cited by 6

WNTers in La Jolla

Sokol, S. Y., & Wharton, K. A. (2007) · Development · doi:10.1242/dev.008169 · Cited by 6

Non-bilayer Lipid Phases Modulate the Structure and Functions of Mitochondrial Membranes: Pharmacological Relevance

Gasanoff (2023) · American Journal of Biomedical Science & Research · doi:10.34297/ajbsr.2023.19.002632 · Cited by 5

Decoding the immune landscape: a comprehensive analysis of immune-associated biomarkers in cervical carcinoma and their implications for immunotherapy strategies

Wang, L., Liu, H., Feng, Y. M., Liu, X., Wang, Y., Liu, Y., Li, H., & Zhang, Y. (2024) · Frontiers in Genetics · doi:10.3389/fgene.2024.1340569 · Cited by 5

Characterization of the oligomerization and ligand-binding properties of recombinant rat lipocalin 11

Gu, Y., Liu, Q., Chen, P., Guo, C., Liu, Y., Zhao, Y., Zhang, Y., & Lin, D. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.08.018 · Cited by 5

Abiotic Stress Tolerance in Plants by Genome Editing Applications

Urhan, E. K. (2023) · Wiley eBooks · doi:10.1002/9781394183913.ch10 · Cited by 5

LCN2-Fungal siderophore-iron binding and uptake leads to oxidative stress and cell death in hepatocellular carcinoma cell line HepG2

Khan, A., Singh, A., Singh, P., Kumar, R. K., Ojha, K. K., Singh, V. K., & Srivastava, A. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2175380 · Cited by 4

Gene Manipulation and Biosynthesis of Phycobiliproteins

Kannaujiya, V. K., Sundaram, S., & Sinha, R. P. (2017) · Springer eBooks · doi:10.1007/978-981-10-6460-9_4 · Cited by 4

Performing training in water improves glucose homeostasis and lipocalins in women with type 2 diabetes mellitus

Bonab, S. B., & Dastah, S. (2022) · Science & Sports · doi:10.1016/j.scispo.2021.08.009 · Cited by 4

Recent Advances on Small-Molecule Inhibitors of Lipocalin-like Proteins

Chen, S., Pan, Z., Liu, M., Guo, L., Jiang, X. L., & He, G. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00086 · Cited by 4

The crystal structure of human protein α1M reveals a chromophore-binding site and two putative protein–protein interfaces

Zhang, Y., Gao, Z., Guo, Z. G., Zhang, H., Zhang, Z., Luo, M., Hou, H., Huang, A., Dong, Y., & Wang, D. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.08.084 · Cited by 4

The investigation of violaxanthin de-epoxidation in the primitive green algaMantoniella squamata(Prasinophyceae) indicates mechanistic differences in xanthophyll conversion to higher plants

Schaller, S., Latowski, D., Jemioła‐Rzemińska, M., Quaas, T., Wilhelm, C., Strzałka, K., & Goss, R. (2012) · Phycologia · doi:10.2216/11-127.1 · Cited by 4

In the matter of Baby Jane Doe: does Reagan really agree with us?

Biklen, D. P., & Ferguson, P. M. (1984) · PubMed · Cited by 4

Function and dynamics of aptamers: A case study on the malachite green aptamer

Wang, T. (2008) · doi:10.31274/etd-180810-93 · Cited by 4

Furry Animal Allergy: Lipocalins, Serum Albumins, and Secretoglobins—Cross-Reactivity, Diagnosis, and Management Strategies

Gromek, W., Kołdej, N., Kurowski, M. M., & Majsiak, E. (2025) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-025-09086-7 · Cited by 5

A disordered region retains the full protease inhibitor activity and the capacity to induce CD8 + T cells in vivo of the oral vaccine adjuvant U-Omp19

Darriba, M. L., Castro, C. P., Coria, L. M., Bruno, L. A., Cerutti, M. L., Otero, L. H., Chemes, L. B., Rasia, R. M., Klinke, S., Cassataro, J., et al. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.08.054 · Cited by 3

β‐Lactoglobulin variants as potential carriers of pramoxine: Comprehensive structural and biophysical studies

Bonarek, P., Mularczyk, D., Loch, J. I., Kurpiewska, K., & Dziedzicka‐Wasylewska, M. (2023) · Journal of Molecular Recognition · doi:10.1002/jmr.3052 · Cited by 3

Identification and characterization of enzymes involved in biosynthesis of different phycobiliproteins in cyanobacteria

Biswas, A. (2011) · ScholarWorks @ The University of New Orleans (The University of New Orleans) · Cited by 3

Solution structure of the protein lipocalin 12 from rat epididymis

Peng, Y., Zhang, X., Liu, J., Liu, Q., Guo, C., Zhang, Y., & Lin, D. (2011) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.23031 · Cited by 3

Molecular Diagnostics in Allergy to Mammals

Hilger, C., Kleine‐Tebbe, J., & van Hage, M. (2017) · Springer eBooks · doi:10.1007/978-3-319-42499-6_19 · Cited by 3

Characterization of Localization, Ligand Binding, and pH-Dependent Conformational Changes of Two Chemosensory Proteins Expressed in the Antennae of the Japanese Carpenter Ant, Camponotus Japonicus

Wen, D., Li, X., Geng, X., Hirai, M., Ajito, S., Takahashi, K., Ozaki, M., Hojo, M., Uebi, T., & Iwasa, T. (2020) · ZOOLOGICAL SCIENCE · doi:10.2108/zs190138 · Cited by 3

Analysis of the testicle’s transcriptome of the Chagas disease vector Rhodnius prolixusPreprint

Cardoso, J. C., Ribeiro, J. M. C., Santos, D. V., Pereira, M. H., Araújo, R. N., Gontijo, N. F., Pessoa, G. C. D., Sant'Anna, M. R. V., Sorgine, M. H. F., Majerowicz, D., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/616193 · Cited by 3

Allergens

Pomés, A., Wünschmann, S., & Chapman, M. D. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-374279-7.16002-3 · Cited by 3

Optimizing lipocalin sequence classification with ensemble deep learning models

Zhang, Y., Yu, L., Xue, L., Liu, F., Jing, R., & Luo, J. (2025) · PLoS ONE · doi:10.1371/journal.pone.0319329 · Cited by 2

Localization and possible function of nrF-AGP, an alpha-1-acid glycoprotein-like protein in viviparous fish Neoditrema ransonnetii (Perciformes, Embiotocidae)

Nakamura, O., Watabe, Y., Matsumoto, N., Takasugi, O., Watanabe, A., & Tsutsui, S. (2014) · Fish Physiology and Biochemistry · doi:10.1007/s10695-014-9978-8 · Cited by 2

Generation of Human Neutrophil Gelatinase-Associated Lipocalin Monoclonal Antibodies for Use in ARCHITECT ® Assay

Hawksworth, D. J., Tu, B., Tieman, B. C., Brophy, S. E., Tyner, J., Muerhoff, A. S., & Ziemann, R. N. (2012) · Hybridoma · doi:10.1089/hyb.2012.0055 · Cited by 2

Molecular cloning and characterization of ClZE, a zeaxanthin epoxidase gene in watermelon (Citrullus lanatus)

Liu, Y., Yao, D., Hu, W., & Duan, H. (2017) · Biotechnology & Biotechnological Equipment · doi:10.1080/13102818.2016.1275803 · Cited by 2

LOPAP (Lonomia obliqua prothrombin activator protease): clonagem e expressão em levedura Pichia pastoris, obtenção de um peptídeo sintético, análise estrutural e avaliação de suas potenciais aplicações.

Carvalho, L. C. C. (2009) · doi:10.11606/t.87.2009.tde-11022010-104758 · Cited by 2

Apolipoprotein M – Studies of Structure and Function

Ahnström, J. (2009) · Lund University Publications (Lund University) · Cited by 2

Structure of SOQ1 lumenal domains identifies potential disulfide exchange for negative regulation of photoprotection, qHPreprint

Yu, G., Pan, X., Hao, J., Shi, L., Zhang, Y., Wang, J., Xiao, Y., Yang, F., Lou, J., Chang, W., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.16.435614 · Cited by 2

Relación de la apolipoproteína D y sus homólogos en Drosophila con las membranas biológicas: Estudio de su función en diferentes procesos celulares y de su localización y efectos sobre las balsas lipídicas

Espinel, M. D. C. (2014) · UVaDOC UVaDOC University of Valladolid Documentary Repository (University of Valladolid) · doi:10.35376/10324/7752 · Cited by 2

An amphipathic helix drives interaction of Fibrillins with plastoglobule lipid dropletsPreprint

Shivaiah, K., Boren, D. M., Herrera-Tequia, A., Vermaas, J. V., & Lundquist, P. K. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.28.559984 · Cited by 2

Characterization of a lipocalin-like molecule from Dermanyssus gallinae as a potential vaccine antigen

Horio, F., Seo, H., Win, S. Y., Sato, J., Motai, Y., Yamagami, S., Sato, T., Ohishi, E., Maekawa, N., Okagawa, T., et al. (2025) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2025.110921 · Cited by 1

Oral Processing of Lipids

Glumac, M., Wang, X., & Chen, J. (2021) · Springer eBooks · doi:10.1007/978-3-030-56909-9_4 · Cited by 2

Molecular cloning of BnZEP and its expression in petals of different colors inBrassica napus L.

JIANG, J., Lushen, T. I. A. N., Guo, S., Yu, Q., Dezhi, Z. E. N. G., & Yingze, N. (2015) · TURKISH JOURNAL OF AGRICULTURE AND FORESTRY · doi:10.3906/tar-1403-17 · Cited by 1

Expression, purification and characterisation of the recombinant possum lipocalin vulpeculin

Lucarelli, V., Colbert, D., Cumming, M. H., Hamiaux, C., Loxley, G. M., Linklater, W. L., Travaš‐Sejdić, J., & Kralicek, A. V. (2022) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2022.130205 · Cited by 1

Interactions of natural products with β-lactoglobulins, members of the lipocalin family

Riihimäki, L. (2009) · Työväentutkimus Vuosikirja · Cited by 1

Mutations Involving RBP4 and SOX3 Underlie Two Novel Forms of Congenital Eye Malformations.

Chou, C. M. (2012) · Deep Blue (University of Michigan) · Cited by 1

Leaving the Fold: Darwin’s Doubt and the Evolution of Protein Folds

Buratovich, M. A. (2015) · Reports - National Center for Science Education (U.S.)

Xanthophyll Cycle in the Light of Thylakoid Membrane Lipids - Membrane Packing, Curvature Elastic Stress and Enzyme Binding

Szilágyi, A. (2007) · Lund University Publications (Lund University)

Significance of G-X-W motif in the myocilin olfactomedin domain

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The Interactions for the RBP Receptor, Stimulated by Retinoic Acid Gene 6

McQuaid, K. (2013) · Maynooth University ePrints and eTheses Archive (Maynooth University)

Vergleichende Untersuchungen zu frühen Wirt-Pathogen-Interaktionen bei akuter und subklinischer Mastitis des Rindes

München, L.-M.-U. (2012)

Molekulare Diagnostik bei Allergie gegen Säugetiere

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Extraction, Purification and partial Characterization of a Carotenoid Binding Protein (CBP) from the Epidermis of the Monarch Butterfly Larvae (Danaus plexippus)

Fang, N. (2016) · FIU - Digital Commons (Florida International University) · doi:10.25148/etd.fidc000724

Proteomics and Transcriptomics of Venomous Animals

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Santiago, P. B. (2016) · doi:10.26512/2015.04.t.24792

Lipocalina bovina e o seu papel na resistência ao carrapato: quantificação em líquidos corporais de raças bovinas com fenótipos contrastantes de infestações com o carrapato Rhipicephalus microplus

de Carvalho, J. A. (2017) · doi:10.11606/d.17.2017.tde-06062017-161955

The methods of particle bombardment and observation of sGFP signals

Wahyudi, A., & Motohashi, R. (2020) · AIP conference proceedings · doi:10.1063/5.0030466

Approche bioinformatique et fonctionnelle pour la caractérisation de protéines sécrétées chez les Trypanosomatidés : implication dans la biologie et la virulence du parasite

Corrales, R. M. (2009) · OpenGrey (Institut de l'Information Scientifique et Technique)

Descrição extensiva dos sialomas de Rhodnius neglectus e Triatoma dimidiata, vetores da doença de Chagas

Santiago, P. B. (2016) · doi:10.26512/2016.t.24792

Peer Review #1 of " Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms (v0.1)"

(2016) · PeerJ · doi:10.7287/peerj.1574v0.1/reviews/1

Peer Review #1 of " Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms (v0.2)"

(2016) · PeerJ · doi:10.7287/peerj.1574v0.2/reviews/1

Peer Review #2 of " Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms (v0.1)"

(2016) · PeerJ · doi:10.7287/peerj.1574v0.1/reviews/2

Allergens

Pomés, A., Wünschmann, S., & Chapman, M. D. (2024) · Elsevier eBooks · doi:10.1016/b978-0-128-24465-4.00028-4

Acute kidney injury markers in pediatric pancreatitis: Differentiating disease states and assessing severity

Garlapally, V., Guo, X., Hornung, L. N., Delgado, K., Cruz‐Monserrate, Z., Safirstein, R. L., Gorelick, F. S., Désir, G. V., Goldstein, S. L., & Abu‐El‐Haija, M. A. (2025) · Journal of Pediatric Gastroenterology and Nutrition · doi:10.1002/jpn3.70285

Rôle des odorants-binding protein dans le mécanisme de transduction olfactive : implication de modifications post-traductionnelles dynamiques dans la spécificité de liaison avec les ligands

Brimau, F. (2010) · doi:10.70675/bfa565a1z6a19z4de2zae33z6376744e0b3e

Rôle de la Sélénoprotéine T dans le remodelage cardiaque post-infarctus et le développement de l'insuffisance cardiaque.

Boukhalfa, I. (2017) · theses.fr (ABES) · doi:10.70675/f17724cbz825ez4a0az9c31z0b10d6d5f706

Role of odorant-binding proteins in Drosophila melanogaster chemosensory perception

Rihani, K. (2019) · theses.fr (ABES) · doi:10.70675/a9a9ebf6z8bf0z4537zaae8zdbdc08eccb5a

The lipocalin protein family: structure and function

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