The DOI matches its Crossref record; 16 of the 17 references it cites were found in a registry or an index.
The three‐dimensional structure of retinol‐binding protein.
Open accessAbstract
The complex of retinol with its carrier protein, retinol-binding protein (RBP) has been crystallized and its three-dimensional structure determined using X-ray crystallography. Its most striking feature is an eight-stranded up-and-down beta barrel core that completely encapsulates the retinol molecule. The retinol molecule lies along the axis of the barrel with the beta-ionone ring innermost and the tip of the isoprene tail close to the surface.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“However, the orientation of retinol in the binding pocket is reversed in relation to that in holo-RBP4 with the β-ionone nearest the mouth of the pocket and the hydroxyl group hydrogen bonding with a Glu residue at the base of the cavity.”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [495]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“all-trans-Retinol is oriented in the binding pocket with its hydroxyl group facing the solvent and the retinyl moiety snuggly bound by a number of nonpolar residues in a highly complementary fashion, explaining the high binding specificity toward the all-trans isomer.”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [495]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The structure of CRBP, similar to that of RBP4, features a β-barrel fold that houses the retinoid-binding site.495”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [495]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“The main structural feature of holo-RBP4, determined crystallographically in the early 1980s, is an eight-stranded β-barrel core containing a single retinol-binding site (Figure 32).495”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [495]
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
The Anatomy and Taxonomy of Protein Structure
Richardson, J. S. (1981) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60520-3 · Cited by 3,378
Blake, C. C. F., Geisow, M. J., Oatley, S. J., Rérat, B., & Rérat, C. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90368-6 · Cited by 792
Winkler, B. (2012) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767312099825 · Cited by 701
Structure of beef liver catalase
Murthy, M. R. N., Reid, T. J. A., Sicignano, A., Tanaka, N., & Rossmann, M. G. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90254-0 · Cited by 428
Orthogonal packing of .beta.-pleated sheets in proteins
Chothia, C., & Janin, J. (1982) · Biochemistry · doi:10.1021/bi00260a009 · Cited by 144
Demonstration in Serum of two Physiological Forms of the Human Retinol Binding Protein*
Peterson, P. A. (1971) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.1971.tb00555.x · Cited by 98
Self-citationThe primary structure of the human retinol‐binding protein
Rask, L., Anundi, H., & Peterson, P. A. (1979) · FEBS Letters · doi:10.1016/0014-5793(79)81084-4 · Cited by 97
Self-citationRask, L., Anundi, H., Böhme, J., Eriksson, U., Fredriksson, A., Nilsson, S. F., Ronne, H., Vahlquist, A., & Peterson, P. A. (1980) · PubMed · Cited by 93
Self-citationSTRUCTURAL AND FUNCTIONAL STUDIES OF VITAMIN A‐BINDING PROTEINS*
Rask, L., Anundi, H., Böhme, J., Eriksson, U., Ronne, H., Sege, K., & Peterson, P. A. (1981) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1981.tb12739.x · Cited by 69
Self-citationShidoji, Y., & Muto, Y. (1977) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)41584-6 · Cited by 69
Research works printed but not linked: 2
- Moore,T. (1972) in Sebrell,W. and Harris,R.S. (eds.), The Vitamins, 1, Academic Press, NY, pp. 245-266.
- Olson,J.A. (1969) Fed. Proc., 28, 1670-1677.
Cited by
Sorted by citations
Items 301–400 of 410
Expression of retinol-binding protein mRNA in mammalian choroid plexus
Duan, W., & Schreiber, G. (1992) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(92)90019-n · Cited by 15
Molecular Mechanisms of Retinoid Function
Redfern, C. P. F. (1997) · Advances in organ biology · doi:10.1016/s1569-2590(08)60052-x · Cited by 15
Pseudo‐homology of protein standard structures formed by two consecutive β‐strands
Efimov, A. V. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)80487-8 · Cited by 15
[19] Purification and properties of plasma retinol-binding protein
Blaner, W. S., & Goodman, D. S. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)89290-x · Cited by 15
Muccio, D. D., Waterhous, D. V., Fish, F., & Brouillette, C. G. (1992) · Biochemistry · doi:10.1021/bi00139a019 · Cited by 15
A novel member of the lipocalin superfamily: tammar wallaby late-lactation protein
Collet, C., & Joseph, R. G. (1993) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(93)90165-6 · Cited by 14
Jang, H. D., & Swaisgood, H. E. (1990) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(90)78886-8 · Cited by 14
Hepatic Retinol Metabolism: Role of the Various Cell Types
Blomhoff, R. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.1987.tb02696.x · Cited by 14
Lipocalins in Arthropod Chemical Communication
Zhu, J., Iannucci, A., Dani, F. R., Knoll, W., & Pelosi, P. (2021) · Genome Biology and Evolution · doi:10.1093/gbe/evab091 · Cited by 13
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
Paulino, M., Esteves, A., Vega, M., Tabarés, G., Ehrlich, R., & Tapia, O. (1998) · Journal of Computer-Aided Molecular Design · doi:10.1023/a:1007938710249 · Cited by 12
Structural changes in retinol binding protein induced by retinol removal. A molecular dynamics study
Sandblom, P., Åqvist, J., Jones, T. A., Newcomer, M. E., A, W. F. V. G., & Tapia, O. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(86)80028-6 · Cited by 12
Self-citationDalgalarrondo, M., Dufour, É., Bertrand-Harb, C., Chobert, J., & Haertlé, T. (1992) · Le Lait · doi:10.1051/lait:199212 · Cited by 12
The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis
Deisenhofer, J., & Michel, H. (1989) · Bioscience Reports · doi:10.1007/bf01117044 · Cited by 12
The homology of complement factor C8 gamma chain and alpha-1-microglobulin
Hunt, L. T., Elżanowski, A., & Barker, W. C. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)91636-6 · Cited by 12
Dufour, É., Dalgalarrondo, M., & Haertlé, T. (1994) · International Journal of Biological Macromolecules · doi:10.1016/0141-8130(94)90009-4 · Cited by 11
The Transthyretin—Retinol-Binding Protein Complex
Monaco, H. L. (2009) · Springer eBooks · doi:10.1007/978-3-642-00646-3_8 · Cited by 12
All fifteen possible arrangements of three disulfide bridges in proteins are known
Warne, N. W., & Laskowski, M. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)91600-w · Cited by 11
Alternative ligands as probes for the carotenoid-binding site of lobster carapace crustacyanin
Clarke, J. B., Eliopoulos, E., Findlay, J. B. C., & Zagalsky, P. F. (1990) · Biochemical Journal · doi:10.1042/bj2650919 · Cited by 11
The size, shape and stability of complement component C9
DiScipio, R. G. (1993) · Molecular Immunology · doi:10.1016/0161-5890(93)90156-6 · Cited by 10
Peptic proteolysis of esterified β‐casein and β‐lactoglobulin
Briand, L. V., Chobert, J., & Haertlé, T. (1995) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1995.tb00579.x · Cited by 10
The Interactions of Water and Proteins in Cellular Function
Watterson, J. G. (1991) · Progress in molecular and subcellular biology · doi:10.1007/978-3-642-76553-7_5 · Cited by 10
The site of linkage of a retinoid affinity label to plasma retinol-binding protein
Gawinowicz, M. A., & Goodman, D. S. (1985) · Journal of Protein Chemistry · doi:10.1007/bf01025298 · Cited by 10
Hydrodynamic and circular dichroic analysis of mammary-derived growth inhibitor (MDGI)
Behlke, J., Mieth, M., Böhmer, F., & Grosse, R. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)91606-9 · Cited by 10
Folli, C., Favilla, R., & Berni, R. (2010) · Methods in molecular biology · doi:10.1007/978-1-60327-325-1_11 · Cited by 9
Regulation of Gene Expression in the Prostate
Matusik, R. J., Cattini, P. A., Leco, K. J., Sheppard, P. C., Nickel, B. E., Neubauer, B. L., Davie, J., Chang, C., Liao, S., Matuo, Y., et al. (1991) · Springer eBooks · doi:10.1007/978-1-4615-3704-5_34 · Cited by 9
Structure et fonction de quelques protéines allergéniques d'origine animale et végétale
Dandeu, J. P., Rabillon, J., & David, B. (1995) · Revue Française d Allergologie et d Immunologie Clinique · doi:10.1016/s0335-7457(05)80367-3 · Cited by 9
Chen, Y., Johnson, C. M., West, K. A., Goldflam, S., Bean, M. F., Huddleston, M. J., Carr, S. A., Gabriel, J. L., & Crabb, J. W. (1994) · Techniques in protein chemistry · doi:10.1016/b978-0-12-194710-1.50046-1 · Cited by 9
Santa, H., Saarela, J. T. A., Laatikainen, R., Rautianen, J., Virtanen, T. I., Rytkönen-Nissinen, M. A., & Mäntyjärvi, R. A. (1998) · Journal of Protein Chemistry · doi:10.1007/bf02780967 · Cited by 8
Bacterial Lipocalins: Origin, Structure, and Function
Akerstrom, B. (2006) · CRC Press eBooks · doi:10.1201/9781498712736-9 · Cited by 8
Der Schlüssel zum Schloß I. Grundlagen der Arzneimittelwirkung
Kubinyi, H. (1994) · Pharmazie in unserer Zeit · doi:10.1002/pauz.19940230307 · Cited by 8
Is the pseudo‐dyad in retroviral proteinase monomers structural or evolutionary?
Rao, J., & Wlodawer, A. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80103-p · Cited by 8
Selvaraj, S. R., Bhatia, V., & Tatu, U. S. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-01-0026 · Cited by 8
Extra- and Intracellular Transport of Retinoids
Eriksson, U. (1990) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4899-1621-1_12 · Cited by 8
Self-citationIntroduction: Overview of the Human Eye, Mammalian Retina, and the Retinoid Visual Cycle
Cioffi, C. L. (2020) · Topics in medicinal chemistry · doi:10.1007/7355_2020_94 · Cited by 7
Reznik, G. O., Yu, Y., Tarr, G. E., & Cantor, C. R. (2003) · Journal of Proteome Research · doi:10.1021/pr0255809 · Cited by 7
Search for the determinants of allergenicity in proteins of the lipocalin family
Rouvinen, J., Virtanen, T. I., & Mäntyjärvi, R. A. (2001) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(01)00109-8 · Cited by 7
Complement component C8γ is expressed in human fetal and adult kidney independent of C8α
Trojer, P., Wojnar, P., Merschak, P., & Redl, B. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00228-8 · Cited by 7
Yu, Y., Zhang, C., Sun, Q., Baral, S., Ding, J., Zhao, F., Yao, Q., Gao, S., Liu, B., & Wang, D. (2024) · Cancer Management and Research · doi:10.2147/cmar.s480337 · Cited by 6
Comparative 17β-estradiol response and lipoprotein interactions of an avian apolipoprotein
Yao, Y., & Vieira, A. V. (2002) · General and Comparative Endocrinology · doi:10.1016/s0016-6480(02)00032-1 · Cited by 6
Molecular and Cellular Biology of Novel Cytoskeletal Proteins in Spermatozoa
Oko, R. J., & Morales, C. R. (1996) · Springer eBooks · doi:10.1007/978-1-4612-2374-0_11 · Cited by 6
Biomaterials for Molecular Electronics Development of Optical Biosensor for Retinol
Ramanathan, K., Švitel, J., Dzgoev, A., Sundaram, P. V., & Danielsson, B. R. G. (2001) · Applied Biochemistry and Biotechnology · doi:10.1385/abab:96:1-3:287 · Cited by 6
High dietary astaxanthin supplementation alters egg yolk nutritional composition in hens
Yu, A.-C., Long, C., Sheng, X., Wang, X., Xiao, L., Chen, X., & Qi, X. (2025) · Poultry Science · doi:10.1016/j.psj.2025.105393 · Cited by 5
Retinoids and retinoid-binding proteins: Unexpected roles in metabolic disease
Blaner, W. S., Paik, J., Brun, P., & Golczak, M. (2024) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2024.10.001 · Cited by 5
Manard, B. T., Jones, S. M. H., & Marcus, R. K. (2014) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201400081 · Cited by 5
The interactions of retinoids with retinol‐binding protein
MANOR, D., Callender, R. H., & Noy, N. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17776.x · Cited by 5
Senak, L., Ju, Z., Noy, N., Callender, R. H., & Manor, D. (1997) · Biospectroscopy · doi:10.1002/(sici)1520-6343(1997)3:2 · Cited by 5
Astalakshmi, P., John, M. B., Kavinilavu, G., & Vimala, D. (2023) · International Journal of Mosquito Research · doi:10.22271/23487941.2023.v10.i4a.680 · Cited by 5
Lipocalines et transport des ligands hydrophobes
Gachon, A. M. (1994) · médecine/sciences · doi:10.4267/10608/2477 · Cited by 5
Wu, C. C., Schrof, W., Lilge, D., Lüddecke, E., & Horn, D. (1990) · Makromolekulare Chemie Macromolecular Symposia · doi:10.1002/masy.19900400116 · Cited by 5
Purification of a Carotenoid‐Binding Protein from the Midgut of the Silkworm, Bombyx mori
Jouni, Z. E., & WELLS, M. (1993) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1993.tb26173.x · Cited by 5
Anticalins in Drug Development
Schlehuber, S., & Skerra, A. (2005) · BioDrugs · doi:10.2165/00063030-200519050-00001 · Cited by 5
Zagalsky, P. F., Mummery, R. S., & WINGER, L. A. (1995) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/0305-0491(94)00160-v · Cited by 5
Klebe, G. (1991) · NATO ASI series. Series B : Physics · doi:10.1007/978-1-4615-3700-7_12 · Cited by 5
Huwe, J. K., Larsen, G. L., & Castellino, S. (1996) · Chemical Research in Toxicology · doi:10.1021/tx9500437 · Cited by 5
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
Modulating Role of TTR in Aβ Toxicity, from Health to Disease
Cardoso, I., Santos, L. M., & Alemi, M. (2016) · InTech eBooks · doi:10.5772/63194 · Cited by 7
Walker, F. A. (2008) · Elsevier eBooks · doi:10.1016/b978-044452839-1.50016-4 · Cited by 4
Findlay, J. B. C., Pappin, D., Brett, M., & Zagalsky, P. F. (1989) · Springer eBooks · doi:10.1007/978-1-4613-0849-2_5 · Cited by 4
Zagalsky, P. F., Mummery, R. S., Eliopoulos, E., & Findlay, J. B. C. (1990) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(90)90131-c · Cited by 4
Purification and properties of porcine allantoic fluid retinol-binding protein
Vallet, J. L. (1996) · Domestic Animal Endocrinology · doi:10.1016/0739-7240(95)00063-1 · Cited by 4
Eriksson, U. (1997) · Progress in Retinal and Eye Research · doi:10.1016/s1350-9462(96)00020-1 · Cited by 3
Self-citationBerni, R., & Lamberti, V. (1989) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(89)90014-x · Cited by 3
Crystallization of P2 myelin protein
Bergfors, T., Sędzik, J., Unge, T., Fridborg, K., Jones, T. A., & Weise, M. J. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90319-6 · Cited by 3
Self-citationMonoclonal antibody studies of the antigenic determinants of human plasma retinol-binding protein
Davila-Bloom, M. E., Blaner, W. S., & Goodman, D. S. (1990) · The Journal of Nutritional Biochemistry · doi:10.1016/0955-2863(90)90077-x · Cited by 3
Sawyer, L. (2002) · Wiley eBooks · doi:10.1002/047120918x.emb0151 · Cited by 3
[28] X-ray crystallographic studies on retinol-binding proteins
Newcomer, M. E., & Jones, T. A. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)89299-w · Cited by 2
Self-citationWang, C., Jiang, S., & Wu, C. (2001) · Macromolecules · doi:10.1021/ma010436e · Cited by 2
Lasker, M. V., Kuruvilla, S. M., Gajjar, M. M., Kapoor, A., & Nair, S. K. (2006) · PubMed Central · Cited by 2
Stamato, F. M. L. G., Paulino, M., Garratt, R. C., Soares, C. M., & Tapia, O. (1995) · Molecular Engineering · doi:10.1007/bf01019470 · Cited by 2
Sacchettini, J. C., Banaszak, L. J., & Gordon, J. I. (1990) · Springer eBooks · doi:10.1007/978-1-4615-3936-0_11 · Cited by 2
Electron Density Fitting with Computer Graphics: A Review and a Glimpse
Jones, T. A. (1987) · Springer eBooks · doi:10.1007/978-1-4684-5272-3_10 · Cited by 2
Self-citationIncorporating Vitamins and Resveratrol into Wines and Tsipouro to Enhance their Antioxidant Capacity
(2024) · Letters in Applied NanoBioScience · doi:10.33263/lianbs134.184 · Cited by 1
Borisenko, A., Bobrysheva, T., Сергеевна, З. М., Anisimov, G. S., Borisenko, A. A., Alexeev, D. G., Razinkova, V., Greseva, E. G., Avanesyan, S. S., Sizonenko, M., et al. (2025) · Food Chemistry Molecular Sciences · doi:10.1016/j.fochms.2025.100261 · Cited by 1
Studies of All- trans Retinoic Acid Transport in the Eye
Chatterjee, S., Roy, A., Yu, J., Read, A. T., Bentley‐Ford, M. R., Pardue, M. T., Kane, M. A., Finn, M. G., & Ethier, C. R. (2025) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.66.6.84 · Cited by 1
X-ray and Neutron Diffraction Approaches to the Structural Analysis of Protein-Lipid Interactions
Hermoso, J. A., Mancheño, J. M., & Pebay‐Peyroula, E. (2006) · Springer eBooks · doi:10.1007/3-540-28435-4_3 · Cited by 1
Zagalsky, P. F., Mummery, R. S., Eliopoulos, E., & Keen, J. N. (1995) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/0305-0491(94)00168-t · Cited by 1
Yamamoto, Y., Yoshizawa, T., Mano, H., Masushige, S., & Kato, S. (1996) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.42.257 · Cited by 1
Napoli, J. L. (2002) · Wiley eBooks · doi:10.1002/0471203076.emm0944 · Cited by 1
PROTEIN UNFOLDING ON INTERFACES: A STRUCTURAL AND FUNCTIONAL STUDY
Miriani, M. (2012) · Archivio Istituzionale della Ricerca (Universita Degli Studi Di Milano) · doi:10.13130/miriani-matteo_phd2012-02-10 · Cited by 1
Molecular Recognition: The Lipocalins
Eliopoulos, E. (1996) · Springer eBooks · doi:10.1007/978-94-009-1692-0_24 · 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
Amoia, A. M. (2006) · UA Campus Repository (The University of Arizona) · Cited by 1
Lazarillo and Related Lipocalins: Ligands and Funcions
García, M. R. (2013) · UVaDOC UVaDOC University of Valladolid Documentary Repository (University of Valladolid) · doi:10.35376/10324/3603 · Cited by 1
Optimum timing for vitamin A supplementation in children with diarrhoea.
Elson, K. I. (2001)
Tailoring Protein Scaffolds for Ligand Recognition
Skerra, A. (2008) · Wiley eBooks · doi:10.1002/9783527610754.ed01
A genetically engineered purpurin/retinol-binding protein hybrid that binds to transthyretin
Melhus, H., & Rask, L. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)90681-a
Self-citationAntigenic determinants of human serum retinol binding protein as probed with monoclonal antibodies
Reddy, B. M. M. M. K., Karande, A. A., & Adiga, P. R. (1993) · Molecular Immunology · doi:10.1016/0161-5890(93)90096-t
Proteomic analysis of human serum from patients with temporal lobe epilepsy
Lee, C. W., Yu, S. T., Choi, H. Y., Koh, B. J., & Kwak, Y. G. (2009) · Korean Journal of Pediatrics · doi:10.3345/kjp.2009.52.5.567
The Interactions for the RBP Receptor, Stimulated by Retinoic Acid Gene 6
McQuaid, K. (2013) · Maynooth University ePrints and eTheses Archive (Maynooth University)
Schlatterer, K., Gminski, R., Schlatterer, J. C., Hecker, E., Chandra, P., Schlatterer, B., Krauter, G., & Chandra, A. (2005) · PubMed
Crystallographic Studies on Retinol-Binding Protein and Beta Lactoglobulin
Monaco, H. L., Zanotti, G., & Spadon, P. (1987) · Humana Press eBooks · doi:10.1007/978-1-4612-4600-8_5
Protein Engineering Studies of ß-Lactoglobulin
Sawyer, L., Morais-Cabral, J. H., & Batt, C. A. (2005) · Elsevier eBooks · doi:10.1533/9780857093066.114
Pancreatic Secretory Trypsin Inhibitor to Rhodopsin Kinase
Haeberli, A. (1998) · Wiley eBooks · doi:10.1002/9783527619764.ch11
Dalton, C. F. (1994) · SHURA (Sheffield Hallam University Research Archive) (Sheffield Hallam University)
Changing the face of craniosynostosis: the role of RBP4 in osteogenesis and suture fusion.
Leitch, V. D. (2011) · Adelaide Research & Scholarship (AR&S) (University of Adelaide)
(1993) · Elsevier eBooks · doi:10.1016/b978-0-12-121070-0.50010-8
Metadata
- Authors
- Newcomer, M. E., Jones, T. A., Aqvist, J., Sundelin, J., Eriksson, U., Rask, L., & Peterson, P. A.
- Affiliations
- Uppsala University (SE)
- Venue
- The EMBO Journal
- Published
- 1984-07-01
- Volume
- 3
- Issue
- 7
- Pages
- 1451-1454
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC557543
- OpenAlex
- W1221193043
- Cited by
- 405
- References
- 17
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 4 · 2023: 1 · 2022: 2 · 2021: 4 · 2020: 5 · 2019: 1 · 2016: 3 · 2015: 5 · 2014: 8 · 2013: 9 · 2012: 3
- FWCI
- 19.55
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Civil War Book Review (submittedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- retinol-binding protein, retinol, vitamin A, protein structure, beta-barrel, protein-ligand complex, beta-ionone ring, crystal structure
- MeSH terms
- Animals, Binding Sites, Humans, Models, Molecular, Protein Conformation, Rabbits, Retinol-Binding Proteins, Vitamin A, X-Ray Diffraction, Rats
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