HCVgp1
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Official Full Name
HCVgp1 polyprotein -
Overview
Hepatitis C Virus is a positive, single stranded RNA virus in the Flaviviridae family. The genome is approximately 10,000 nucleotides and encodes a single polyprotein of about 3,000 amino acids. The polyprotein is processed by host cell and viral proteases into three major structural proteins and several non structural proteins necessary for viral replication. Several different genotypes of HCV with slightly different genomic sequences have since been identified that correlate with differences in response to treatment with interferon alpha. -
Synonyms
HCVgp1;HCVgp1 polyprotein
Recombinant Proteins
- HCV
- E.coli
- Non
- β-gal
- His
- GST
Involved Pathway
HCVgp1 involved in several pathways and played different roles in them. We selected most pathways HCVgp1 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with HCVgp1 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|
Protein Function
HCVgp1 has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by HCVgp1 itself. We selected most functions HCVgp1 had, and list some proteins which have the same functions with HCVgp1. You can find most of the proteins on our site.
| Function | Related Protein |
|---|
Interacting Protein
HCVgp1 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with HCVgp1 here. Most of them are supplied by our site. Hope this information will be useful for your research of HCVgp1.
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References
- Tang, Y; Diao, Y; et al. Isolation and Genetic Characterization of a Tembusu Virus Strain Isolated From Mosquitoes in Shandong, China. TRANSBOUNDARY AND EMERGING DISEASES 62:209-216(2015).
- Deshmukh, L; Ghirlando, R; et al. Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 112:3374-3379(2015).
