A Turn-like Structure “KKPE” Segment Mediates the Specific Binding of Viral Protein A27 to Heparin and Heparan Sulfate on Cell Surfaces-Reference-Cited by-同舟云学术

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A Turn-like Structure “KKPE” Segment Mediates the Specific Binding of Viral Protein A27 to Heparin and Heparan Sulfate on Cell Surfaces

Published:2009-12 Issue:52 Volume:284 Page:36535-36546
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Shih Ping-Chen,Yang Min-Shiang,Lin Su-Ching,Ho Yu,Hsiao Jye-Chian,Wang Da-Rong,Yu Steve S.-F.,Chang Wen,Tzou Der-Lii M.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference43 articles.

1. The complete DNA sequence of vaccinia virus

2. Fields Virology;Moss,2007

3. In A Nutshell: Structure and Assembly of the Vaccinia Virion

4. Disulfide Bond Formation at the C Termini of Vaccinia Virus A26 and A27 Proteins Does Not Require Viral Redox Enzymes and Suppresses Glycosaminoglycan-Mediated Cell Fusion

5. The Envelope G3L Protein Is Essential for Entry of Vaccinia Virus into Host Cells

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1. Discovery of a Heparan-Sulfate Binding Domain in Monkeypox Virus H3 Protein as a New Anti-poxviral Drug Target;2024-08-13

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4. Exploring monkeypox virus proteins and rapid detection techniques;Frontiers in Cellular and Infection Microbiology;2024-05-28

5. Kinetic and Structural Aspects of Glycosaminoglycan–Monkeypox Virus Protein A29 Interactions Using Surface Plasmon Resonance;Molecules;2022-09-11

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