Cited by 410Enzyme Structure and FunctionRetinoids in leukemia and cellular processesProtein Structure and Dynamics

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 access

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.xPMC PMC557543

Open this paper in CoChat — free account Open PDF

Abstract

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.

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

Crossref · 10.1002/j.1460-2075.1984.tb01995.x

Cites

16 of 16 references verified0 citation errors · 0 not checkable

Statistics

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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
Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å
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
Computational crystallography
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-citation
The 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-citation
The retinol-binding protein.
Rask, 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-citation
STRUCTURAL 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-citation
Vitamin A transport in plasma of the non-mammalian vertebrates: isolation and partial characterization of piscine retinol-binding protein
Shidoji, Y., & Muto, Y. (1977) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)41584-6 · Cited by 69

Show all 17 references

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.

Sorted by citations

Items 101–200 of 410

Characterization of the gene encoding ovine beta-lactoglobulin
Ali, S., & Clark, A. J. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90614-6 · Cited by 116
Das photosynthetische Reaktionszentrum des Purpurbakteriums Rhodopseudomonas viridis (Nobel‐Vortrag)
Deisenhofer, J., & Michel, H. (1989) · Angewandte Chemie · doi:10.1002/ange.19891010705 · Cited by 115
A novel type of receptor protein, based on the lipocalin scaffold, with specificity for digoxigenin11Edited by R. Huber
Schlehuber, S., Beste, G., & Skerra, A. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3646 · Cited by 115
The Transfer of Retinol from Serum Retinol-binding Protein to Cellular Retinol-binding Protein Is Mediated by a Membrane Receptor
Sundaram, M., Sivaprasadarao, A., DeSousa, M. M., & Findlay, J. B. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3336 · Cited by 111
β‐Lactoglobulin binds retinol and protoporphyrin IX at two different binding sites
Dufour, É., Marden, M. C., & Haertlé, T. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80850-i · Cited by 110
Similarities and differences between human cyclophilin A and other β-barrel structures
Ke, H. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90841-7 · Cited by 110
Retinoids and Retinal Diseases
Kiser, P. D., & Palczewski, K. (2016) · Annual Review of Vision Science · doi:10.1146/annurev-vision-111815-114407 · Cited by 108
“A single ROL-binding site is formed by the core, eight-stranded, β-barrel fold of RBP4 (Figure 9a) (Newcomer et al. 1984).”
Human Apolipoprotein D Gene: Gene Sequence, Chromosome Localization, and Homology to the α 2u -Globulin Superfamily
Drayna, D. T., McLEAN, J. W., Wion, K. L., Trent, J. M., Drabkin, H. A., & Lawn, R. M. (1987) · DNA · doi:10.1089/dna.1987.6.199 · Cited by 106
Retinol is essential for growth of activated human B cells.
Buck, J., Ritter, G., Dannecker, L., Katta, V., Cohen, S. L., Chait, B. T., & Hämmerling, U. (1990) · The Journal of Experimental Medicine · doi:10.1084/jem.171.5.1613 · Cited by 105
Refined apoprotein structure of rat intestinal fatty acid binding protein produced in Escherichia coli.
Sacchettini, J. C., Gordon, J. I., & Banaszak, L. J. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.20.7736 · Cited by 104
Molecular properties of bovine interphotoreceptor retinol-binding protein.
Adler, A. J., Evans, C. D., & Stafford, W. F. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89149-9 · Cited by 104
The crystal structure of nitrophorin 4 at 1.5 å resolution: transport of nitric oxide by a lipocalin-based heme protein
Andersen, J. F., Weichsel, A., Balfour, C. A., Champagne, D. E., & Montfort, W. R. (1998) · Structure · doi:10.1016/s0969-2126(98)00131-2 · Cited by 103
Cellular localization of apolipoprotein D and lecithin:cholesterol acyltransferase mRNA in rhesus monkey tissues by in situ hybridization.
Smith, K., Lawn, R. M., & Wilcox, J. (1990) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)42739-7 · Cited by 103
Signaling by vitamin A and retinol-binding protein in regulation of insulin responses and lipid homeostasis
Berry, D. C., & Noy, N. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2011.07.002 · Cited by 100
Crystal structure of a secondary vitamin D 3 binding site of milk β‐lactoglobulin
Yang, M., Guan, H., Liu, M., Lin, Y.-H., Yang, J., Chen, W., Chen, C., & Mao, S. J. T. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21811 · Cited by 100
The retinal pigment epithelial membrane receptor for plasma retinol-binding protein. Isolation and cDNA cloning of the 63-kDa protein.
Båvik, C., Lévy, F., Hellman, U., Wernstedt, C., & Eriksson, U. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80759-5 · Cited by 100
Self-citation
Crystal structures of bovine beta-lactoglobulin in the orthorhombic space group C2221 . Structural differences between genetic variants A and B and features of the Tanford transition
Oliveira, K. M. G., Valente‐Mesquita, V. L., Caarls, M. B., Sawyer, L., Ferreira, S. T., & Polikarpov, I. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2001.01918.x · Cited by 99
The Menagerie of Human Lipocalins: A Natural Protein Scaffold for Molecular Recognition of Physiological Compounds
Schiefner, A., & Skerra, A. (2015) · Accounts of Chemical Research · doi:10.1021/ar5003973 · Cited by 97
Interactions amongst plasma retinol-binding protein, transthyretin and their ligands: implications in vitamin A homeostasis and transthyretin amyloidosis
Pullakhandam, R., & Sivakumar, B. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.09.023 · Cited by 100
Prediction of protein helix content from an autocorrelation analysis of sequence hydrophobicities
Horne, D. S. (1988) · Biopolymers · doi:10.1002/bip.360270308 · Cited by 96
cDNA Cloning and Sequencing Reveal the Major Horse Allergen Equ c1 to Be a Glycoprotein Member of the Lipocalin Superfamily
Grégoire, C., Rosinski‐Chupin, I., Rabillon, J., Alzari, P. M., David, B., & Dandeu, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.51.32951 · Cited by 94
The xanthophyll cycle - molecular mechanism and physiological significance
Latowski, D., Grzyb, J., & Strzałka, K. (2004) · Acta Physiologiae Plantarum · doi:10.1007/s11738-004-0009-8 · Cited by 93
Experimentally determined lipocalin structures
Flower, D. R. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00147-3 · Cited by 91
Comparison of the ligand binding properties of two homologous rat apocellular retinol-binding proteins expressed in Escherichia coli.
Levin, M. S., Locke, B., Yang, N. C., Li, E., & Gordon, J. I. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77895-8 · Cited by 91
Intracellular Fatty-Acid-Binding Proteins Characteristics and Function
Paulussen, R. J. A., & Veerkamp, J. H. (1990) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4899-1621-1_7 · Cited by 91
Biosynthesis, Absorption, Metabolism and Transport of Retinoids
Vogel, S., Gamble, M. V., & Blaner, W. S. (1999) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-58483-1_2 · Cited by 91
The solution structure and dynamics of human neutrophil gelatinase-associated lipocalin 1 1Edited by A. R. Fersht
Coles, M. P., Diercks, T., Muehlenweg, B., Bartsch, S., Zoelzer, V., Tschesche, H., & Kessler, H. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2755 · Cited by 88
Molecular mechanisms of olfaction.
Snyder, S. H., Sklar, P. B., & Pevsner, J. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68169-4 · Cited by 87
Structure of the lamprey yolk lipid-protein complex lipovitellin-phosvitin at 2.8 Å resolution
Raag, R., Appelt, K., Xuong, N., & Banaszak, L. J. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90542-6 · Cited by 87
Structure and cell‐specific expression of a cloned human retinol binding protein gene: the 5′‐flanking region contains hepatoma specific transcriptional signals.
D’Onofrio, C., Colantuoni, V., & Cortese, R. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03881.x · Cited by 87
Retinoid‐binding proteins: structural determinants important for function
Newcomer, M. E. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.2.7781925 · Cited by 86
Self-citation
Binding of retinoids and β-carotene to β-lactoglobulin. Influence of protein modifications
Dufour, É., & Haertlé, T. (1991) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(91)90075-b · Cited by 85
The primary structure of rabbit and rat prealbumin and a comparison with the tertiary structure of human prealbumin.
Sundelin, J., Melhus, H., Das, S., Eriksson, U., Lind, P., Trägårdh, L., Peterson, P. A., & Rask, L. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)88997-9 · Cited by 85
Self-citation
Structure of the epididymal retinoic acid binding protein at 2.1 Å resolution
Newcomer, M. E. (1993) · Structure · doi:10.1016/0969-2126(93)90004-z · Cited by 84
Self-citation
Crystal Structure of the Allergen Equ c 1
Lascombe, M., Grégoire, C., Poncet, P., Tavares, G., Rosinski‐Chupin, I., Rabillon, J., Goubran‐Botros, H., Mazié, J. C., David, B., & Alzari, P. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002854200 · Cited by 84
Identification and Characterization of a Non-retinoid Ligand for Retinol-binding Protein 4 Which Lowers Serum Retinol-binding Protein 4 Levels in Vivo
Motani, A. S., Wang, Z., Conn, M. T., Siegler, K., Zhang, Y., Liu, Q., Johnstone, S., Xu, H., Thibault, S., Wang, Y., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809654200 · Cited by 83
Sequence analysis, cellular localization, and expression of a neuroretina adhesion and cell survival molecule
Berman, P. W., Gray, P., Chen, E., Keyser, K. T., Ehrlich, D., Karten, H. J., LaCorbiere, M., Esch, F. S., & Schubert, D. A. (1987) · Cell · doi:10.1016/0092-8674(87)90018-3 · Cited by 82
New Approaches And Concepts in The Study of Differentiation of Oral Epithelia
Dale, B. A., Salonen, J. I., & Jones, A. H. (1990) · Critical Reviews in Oral Biology & Medicine · doi:10.1177/10454411900010030201 · Cited by 81
Hydrolysis of β‐lactoglobulin by thermolysin and pepsin under high hydrostatic pressure
Dufour, É., Hervé, G., & Haertlé, T. (1995) · Biopolymers · doi:10.1002/bip.360350506 · Cited by 80
The primary structure of aphrodisin.
Henzel, W. J., Rodriguez, H., Singer, A. G., Stults, J. T., Macrides, F., Agosta, W. C., & Niall, H. D. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37444-1 · Cited by 80
Apolipoprotein D transcription occurs specifically in nonproliferating quiescent and senescent fibroblast cultures
Provost, P. R., Marcel, Y. L., Milne, R. W., WEECH, P. K., & Rassart, É. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)81244-3 · Cited by 78
Binding of p-Nitrophenyl Phosphate and Other Aromatic Compounds by β-Lactoglobulin
Farrell, H. M., Behe, M. J., & Enyeart, J. A. (1987) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(87)80004-8 · Cited by 77
Acute Phase Proteins and Their Role in Periodontitis: A Review
Polepalle, T. (2015) · JOURNAL OF CLINICAL AND DIAGNOSTIC RESEARCH · doi:10.7860/jcdr/2015/15692.6728 · Cited by 76
Characterization of disulfide-linked heterodimers containing apolipoprotein D in human plasma lipoproteins.
Blanco-Vaca, F., Via, D., Yang, C., Massey, J., & Pownall, H. (1992) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)41336-7 · Cited by 68
Stationary Phase Expression of a Novel Escherichia coli Outer Membrane Lipoprotein and Its Relationship with Mammalian Apolipoprotein D
Bishop, R. E., Penfold, S. S., Frost, L. S., Höltje, J., & Weiner, J. H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.39.23097 · Cited by 76
Identification, characterization, and tissue distribution of apolipoprotein D in the rat.
Boyles, J. K., Notterpek, L. M., Wardell, M. R., & Rall, S. C. (1990) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)42112-1 · Cited by 76
Amino acid sequence homologies between rabbit, rat, and human serum retinol-binding proteins.
Sundelin, J., Laurent, B. C., Anundi, H., Trägårdh, L., Larhammar, D., Björck, L., Eriksson, U., Åkerström, B., Jones, A. G., & Newcomer, M. E. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)88996-7 · Cited by 75
Self-citation
Vitamin A Transport Mechanism of the Multitransmembrane Cell-Surface Receptor STRA6
Kawaguchi, R., Zhong, M., Kassai, M., Ter-Stepanian, M., & Sun, H. (2015) · Membranes · doi:10.3390/membranes5030425 · Cited by 75
Retinoid Homeostasis and Beyond: How Retinol Binding Protein 4 Contributes to Health and Disease
Steinhoff, J. S., Lass, A., & Schupp, M. (2022) · Nutrients · doi:10.3390/nu14061236 · Cited by 79
Primary structure of a photoactive yellow protein from the phototrophic bacterium Ectothiorhodospira halophila, with evidence for the mass and the binding site of the chromophore
BEEUMEN, J. V., Devreese, B. V., Bun, S. M. V., Hoff, W. D., Hellingwerf, K. J., Meyer, T. E., Cusanovich, M. A., & McRee, D. E. (1993) · Protein Science · doi:10.1002/pro.5560020706 · Cited by 73
Molecular characterization and differential mRNA tissue distribution of mouse apolipoprotein D
Séguin, D., Desforges, M., & Rassart, É. (1995) · Molecular Brain Research · doi:10.1016/0169-328x(95)00008-g · Cited by 73
Complete assignment of 1H, 13C and 15N chemical shifts for bovine β-lactoglobulin: Secondary structure and topology of the native state is retained in a partially unfolded form
Uhrı́nová, S., Uhrı́n, D., Denton, H., Smith, M. H., Sawyer, L., & Barlow, P. N. (1998) · Journal of Biomolecular NMR · doi:10.1023/a:1008268528695 · Cited by 73
Folding of a predominantly .beta.-structure protein: rat intestinal fatty acid binding protein
Ropson, I. J., Gordon, J. I., & Frieden, C. (1990) · Biochemistry · doi:10.1021/bi00493a013 · Cited by 73
Retinoid binding to retinol-binding protein and the interference with the interaction with transthyretin
Malpeli, G., Folli, C., & Berni, R. (1996) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(95)00264-2 · Cited by 74
Crystal Structure of the Dog Lipocalin Allergen Can f 2: Implications for Cross-reactivity to the Cat Allergen Fel d 4
Madhurantakam, C., Nilsson, O. B., Uchtenhagen, H., Konradsen, J. R., Saarne, T., Högbom, E., Sandalova, T., Grönlund, H., & Achour, A. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.05.043 · Cited by 70
A structural basis of light energy and electron transfer in biology
Huber, R. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb15305.x · Cited by 70
Studies of the Fatty Acid-binding Site of Rat Liver Fatty Acid-binding Protein Using Fluorescent Fatty Acids
Storch, J., Bass, N. M., & Kleinfeld, A. M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81850-6 · Cited by 70
The architecture of invertebrate carotenoproteins
Zagalsky, P. F., Eliopoulos, E., & Findlay, J. B. C. (1990) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(90)90171-o · Cited by 69
‘Anticalins’: a new class of engineered ligand-binding proteins with antibody-like properties
Skerra, A. (2001) · Reviews in Molecular Biotechnology · doi:10.1016/s1389-0352(01)00020-4 · Cited by 67
Gastrotropin: not an enterooxyntin but a member of a family of cytoplasmic hydrophobic ligand binding proteins
Gantz, I., Nothwehr, S. F., Lucey, M. R., Sacchettini, J. C., DelValle, J., Banaszak, L. J., Naud, M., Gordon, J. I., & Yamada, T. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47054-3 · Cited by 67
Milk Processing Affects Structure, Bioavailability and Immunogenicity of β-lactoglobulin
Broersen, K. (2020) · Foods · doi:10.3390/foods9070874 · Cited by 66
Tissue distribution of the receptor for plasma retinol-binding protein
Smeland, S., Bjerknes, T., Malaba, L. C., Eskild, W., Norum, K. R., & Blomhoff, R. (1995) · Biochemical Journal · doi:10.1042/bj3050419 · Cited by 66
Structure and function of the porin channel
Welte, W., Nestel, U., Wacker, T., & Diederichs, K. (1995) · Kidney International · doi:10.1038/ki.1995.374 · Cited by 66
Complete sequence and model for the A2 subunit of the carotenoid pigment complex, crustacyanin
Keen, J. N., CACERES, I., Eliopoulos, E., Zagalsky, P. F., & Findlay, J. B. C. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb15925.x · Cited by 66
Nobel lecture. A structural basis of light energy and electron transfer in biology.
Huber, R. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08337.x · Cited by 66
A chemistry of mammalian pheromones
Singer, A. G. (1991) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/0960-0760(91)90261-3 · Cited by 66
Comparative molecular modelling of the Fas-ligand and other members of the TNF family
Peitsch, M. C., & Tschopp, J. (1995) · Molecular Immunology · doi:10.1016/0161-5890(95)00016-8 · Cited by 66
Characterization of two post-translationally processed forms of human serum retinol-binding protein: altered ratios in chronic renal failure.
Jaconi, S., Rose, K., Hughes, G. J., Saurat, J. ‐., & Siegenthaler, G. (1995) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)41132-0 · Cited by 65
Localization of the major sites of rabbit apolipoprotein D gene transcription by in situ hybridization.
Provost, P. R., Villeneuve, L., WEECH, P. K., Milne, R. W., Marcel, Y. L., & Rassart, É. (1991) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)41899-1 · Cited by 65
Reversible effects of medium dielectric constant on structural transformation of β‐lactoglobulin and its retinol binding
Dufour, É., Bertrand-Harb, C., & Haertlé, T. (1993) · Biopolymers · doi:10.1002/bip.360330408 · Cited by 63
Ligand-Binding Study of Anopheles gambiae Chemosensory Proteins
Iovinella, I., Bozza, F., Caputo, B., della Torre, A., & Pelosi, P. (2013) · Chemical Senses · doi:10.1093/chemse/bjt012 · Cited by 62
Protein synthesis at the blood-brain barrier. The major protein secreted by amphibian choroid plexus is a lipocalin
Achen, M. G., Harms, P. J., Thomas, T., Richardson, S. J., Wettenhall, R. E. H., & Schreiber, G. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50072-7 · Cited by 62
Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by solid-state deuterium NMR
Ulrich, A. S., Heyn, M. P., & Watts, A. G. (1992) · Biochemistry · doi:10.1021/bi00157a029 · Cited by 61
The membrane bound bacterial lipocalin Blc is a functional dimer with binding preference for lysophospholipids
Campanacci, V., Bishop, R. E., Blangy, S., Tegoni, M., & Cambillau, C. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.07.086 · Cited by 59
Structural Mechanism of Specific Ligand Recognition by a Lipocalin Tailored for the Complexation of Digoxigenin
Korndörfer, I. P., Schlehuber, S., & Skerra, A. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00573-4 · Cited by 59
Surface fractality as a guide for studying protein-protein interactions
Åqvist, J., & Tapia, O. (1987) · Journal of Molecular Graphics · doi:10.1016/0263-7855(87)80042-5 · Cited by 58
Sensitive ECL immunosensor for detection of retinol-binding protein based on double-assisted signal amplification strategy of multiwalled carbon nanotubes and Ru(bpy)32+ doped mesoporous silica nanospheres
Wu, B., Hu, C., Hu, X., Cao, H., Huang, C., Shen, H., & Jia, N. (2013) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2013.06.045 · Cited by 57
Crystallographic structure of a photoreceptor protein at 2.4 A resolution.
McRee, D. E., Tainer, J. A., Meyer, T. E., BEEUMEN, J. V., Cusanovich, M. A., & Getzoff, E. D. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.17.6533 · Cited by 57
Molecular dynamics simulations of the holo and apo forms of retinol binding protein
Åqvist, J., Sandblom, P., Jones, T. A., Newcomer, M. E., A, W. F. V. G., & Tapia, O. (1986) · Journal of Molecular Biology · doi:10.1016/0022-2836(86)90279-2 · Cited by 57
Self-citation
Design, Synthesis, and Evaluation of Nonretinoid Retinol Binding Protein 4 Antagonists for the Potential Treatment of Atrophic Age-Related Macular Degeneration and Stargardt Disease
Cioffi, C. L., Dobri, N., Freeman, E. E., Conlon, M. P., Chen, P., Stafford, D. G., Schwarz, D. M. C., Golden, K. C., Zhu, L., Kitchen, D. B., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm5010013 · Cited by 57
Molecular characterization and differential mRNA tissue distribution of rabbit apolipoprotein D.
Provost, P. R., WEECH, P. K., Tremblay, N., Marcel, Y. L., & Rassart, É. (1990) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)42270-9 · Cited by 55
Crystallographic studies on complexes between retinoids and plasma retinol-binding protein.
Zanotti, G., Marcello, M., Malpeli, G., Folli, C., Sartori, G., & Berni, R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43925-7 · Cited by 54
Structure and chromosomal localization of the human gene for a brain form of prostaglandin D2 synthase
White, D. M., Mikol, D. D., Espinosa, R., Weimer, B. C., Beau, M. M. L., & Stefánsson, K. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50077-6 · Cited by 53
Characterization of a cloned cDNA encoding rabbit myelin P2 protein.
Narayanan, V., Barbosa, E., Reed, R. R., & Tennekoon, G. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68481-9 · Cited by 53
The crystal structure of the Escherichia coli lipocalin Blc suggests a possible role in phospholipid binding
Campanacci, V., Nurizzo, D., Spinelli, S., Valencia, C., Tegoni, M., & Cambillau, C. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00199-1 · Cited by 52
Expression of rat intestinal fatty acid binding protein in E. coli and its subsequent structural analysis: a model system for studying the molecular details of fatty acid-protein interaction
Sacchettini, J., Banaszak, L. J., & Gordon, J. (1990) · Molecular and Cellular Biochemistry · doi:10.1007/bf00231371 · Cited by 52
Insights into the role of bacteria in vitamin A biosynthesis: Future research opportunities
Srinivasan, K., & Buys, E. M. (2019) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2018.1546670 · Cited by 53
Cellular retinoid binding proteins
Sundelin, J., Eriksson, U., Melhus, H., NILSSON, M. H. L., Lundvall, J., Båvik, C., Hansson, E., Laurent, B. C., & Peterson, P. A. (1985) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(85)90065-9 · Cited by 51
Self-citation
Estrogen Regulation of Gene Transcription and mRNA Stability
Shapiro, D. J., Barton, M. C., Mckearin, D. M., Chang, T., Lew, D., Blume, J. E., Nielsen, D. A., & Gould, L. J. (1989) · Elsevier eBooks · doi:10.1016/b978-0-12-571145-6.50006-6 · Cited by 51
Structure and expression of the rat epididymal secretory protein I gene. An androgen-regulated member of the lipocalin superfamily with a rare splice donor site
Girotti, M., Jones, R., Emery, D. C., Chia, W., & Hall, L. N. (1992) · Biochemical Journal · doi:10.1042/bj2810203 · Cited by 50
Studies of the spontaneous transfer of retinol from the retinol: retinol-binding protein complex to unilamellar liposomes
Fex, G. A., & Johannesson, G. (1987) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(87)90122-2 · Cited by 49
Complete sequence and model for the C1 subunit of the carotenoprotein crustacyanin, and model for the dimer, β‐crustacyanin, formed from the C1 and A2 subunits with astaxanthin
Keen, J. N., CACERES, I., Eliopoulos, E., Zagalsky, P. F., & Findlay, J. B. C. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16340.x · Cited by 49
The Ile-84–>Ser amino acid substitution in transthyretin interferes with the interaction with plasma retinol-binding protein.
Berni, R., Malpeli, G., Folli, C., Murrell, J. R., Liepnieks, J. J., & Benson, M. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31527-2 · Cited by 49
Cloning and sequencing of a full length cDNA corresponding to human cellular retinol-binding protein
Colantuoni, V., Cortese, R., NILSSON, M. H. L., Lundvall, J., Båvik, C., Eriksson, U., Peterson, P. A., & Sundelin, J. (1985) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(85)90435-8 · Cited by 49
Self-citation
Transmembrane β-barrel proteins
Schulz, G. E. (2003) · Advances in protein chemistry · doi:10.1016/s0065-3233(03)63003-2 · Cited by 48
Three‐dimensional structure and active site of three hydrophobic molecule‐binding proteins with significant amino acid sequence similarity
Monaco, H. L., & Zanotti, G. (1992) · Biopolymers · doi:10.1002/bip.360320425 · Cited by 48
Characterization of the rat retinol-binding protein gene and its comparison to the three-dimensional structure of the protein.
Laurent, B. C., NILSSON, M. H. L., Båvik, C., Jones, T. A., Sundelin, J., & Peterson, P. A. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39053-1 · Cited by 48
Self-citation
CRYSTALLOGRAPHIC STUDIES ON COMPLEXES BETWEEN RETINOIDS AND PLASMA RETINOL-BINDING PROTEIN
Zanotti, G., Marcello, M., Malpeli, G., Sartori, G., & Berni, R. (1994) · Worldwide Protein Data Bank · doi:10.2210/pdb1fem/pdb · Cited by 48
β-Lactoglobulin
Sawyer, L. (2003) · Springer eBooks · doi:10.1007/978-1-4419-8602-3_7 · Cited by 47
Binding of benzo(α)pyrene, ellipticine, and cis-parinaric acid to β-lactoglobulin: Influence of protein modifications
Dufour, É., Roger, P., & Haertlé, T. (1992) · Journal of Protein Chemistry · doi:10.1007/bf01024965 · Cited by 47

Authors: Newcomer, M. E., Jones, T. A., Aqvist, J., Sundelin, J., Eriksson, U., Rask, L., & Peterson, P. A.
Affiliations: Uppsala University (SE)
ORCID: Newcomer, M.E.
Jones, T.A.
Eriksson, U.
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 1984-07-01
Volume: 3
Issue: 7
Pages: 1451-1454
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1002/j.1460-2075.1984.tb01995.x
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
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
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

The three‐dimensional structure of retinol‐binding protein.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks