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Cited by 309

The DOI matches its Crossref record; 88 of the 88 references it cites were found in a registry or an index.

Crystallographic refinement of human serum retinol binding protein at 2Å resolution

Cowan, Sandra W., Newcomer, Marcia E., Jones, T. Alwyn·1990·Proteins: Structure, Function, and Bioinformatics

Abstract

Human serum retinol binding protein (RBP) in complex with retinol has been crystallographically refined to an R‐factor of 18.1% with 2Å resolution data. The protein topology results in an anti‐parallel β‐barrel that encapsulates the retinol ligand. A detailed description of the protein and the binding site is provided. Our structural work has helped to define a family of proteins, many of which are carrier proteins for smaller ligand molecules. We describe the structural basis for the conservation of sequence within the family.

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Crossref · 10.1002/prot.340080108

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Metadata

Authors
Cowan, S. W., Newcomer, M. E., & Jones, T. A.
Venue
Proteins: Structure, Function, and Bioinformatics
Publisher
Wiley
Published
1990-01
Volume
8
Issue
1
Pages
44-61
ISSN
  • 0887-3585 (ISSN-L)
  • 1097-0134
OpenAlex
W2136008324
Cited by
309
References
88
FWCI
15.35
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Crystallographic refinement of human serum retinol binding protein at 2Å resolution. https://app.cochat.ai/papers/10.1002/prot.340080108
The paper
Cowan, S. W., Newcomer, M. E., & Jones, T. A. (1990). Crystallographic refinement of human serum retinol binding protein at 2Å resolution. Proteins: Structure, Function, and Bioinformatics. https://doi.org/10.1002/prot.340080108

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.