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Cited by 551

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Proline-Dependent Structural and Biological Properties of Peptides and Proteins

Yaron, Arieh, Naider, Fred, Scharpe, S.·1993·Critical Reviews in Biochemistry and Molecular Biology

Abstract

Proline residues confer unique structural constraints on peptide chains and markedly influence the susceptibility of proximal peptide bonds to protease activity. This review presents a critical analysis of peptidases involved in the cleavage of proline-containing peptide bonds, with particular attention to the role of proline peptidases in the regulation of the lifetime of biologically active peptides. Peptidases discussed include aminopeptidase P, prolidase, dipeptidyl peptidase IV, prolyl endopeptidase, and prolyl iminopeptidase. Attention is also given to HIV-1 protease, because this key enzyme processes an Xaa-Pro peptide bond. Analysis of the above enzymes reveals that they may function as key pacemakers in the control of the activity of many peptide hormones and that they are involved in a variety of immunological processes, including T-cell-mediated immune response. The novel occurrence of cis-trans isomerization about Xaa-Pro bonds and the biological function of peptidyl-prolyl cis-trans isomerases (immunophilins) are reviewed.

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Metadata

Authors
Yaron, A., Naider, F., & Scharpe, S.
Venue
Critical Reviews in Biochemistry and Molecular Biology
Published
1993-01
Volume
28
Issue
1
Pages
31-81
ISSN
  • 0045-6411 (ISSN-L)
  • 1040-9238
  • 1549-7798
OpenAlex
W2162061338
Cited by
551
References
5
FWCI
2.11
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Proline-Dependent Structural and Biological Properties of Peptides and Proteins. https://app.cochat.ai/papers/10.3109/10409239309082572
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Yaron, A., Naider, F., & Scharpe, S. (1993). Proline-Dependent Structural and Biological Properties of Peptides and Proteins. Critical Reviews in Biochemistry and Molecular Biology. https://doi.org/10.3109/10409239309082572

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