N-Gemini peptides: cytosolic protease resistance via N-terminal dimerization of unstructured peptides-Reference-Cited by-同舟云学术

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N-Gemini peptides: cytosolic protease resistance via N-terminal dimerization of unstructured peptides

Published:2018 Issue:2 Volume:54 Page:204-207
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Fayer Effrat L.¹²³⁴⁵,Gilliland William M.¹²³⁴⁵,Ramsey J. Michael¹²³⁴⁵^ORCID,Allbritton Nancy L.¹²³⁴⁵^ORCID,Waters Marcey L.¹²³⁴⁵^ORCID

Affiliation:

1. Department of Chemistry

2. CB 3290

3. University of North Carolina at Chapel Hill

4. Chapel Hill

5. USA

Abstract

N-Terminal dimerization is a synthetically straight-forward strategy to provide protease resistance to unstructured peptides while maintaining their biological function.

Funder

National Institute of Biomedical Imaging and Bioengineering

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2018/CC/C7CC06819K

Reference37 articles.

1. A Giant Protease with Potential to Substitute for Some Functions of the Proteasome

2. Tripeptidyl peptidases: enzymes that count

3. Major Histocompatibility Complex Class I-presented Antigenic Peptides Are Degraded in Cytosolic Extracts Primarily by Thimet Oligopeptidase

4. Prolyl Oligopeptidase

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