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Membrane interaction of segment H1 (NS4B(H1)) from hepatitis C virus non-structural protein 4B

Biochimica Et Biophysica Acta

Jan 5, 2011

M Francisca Palomares-Jerez, José Villalaín

Abstract

NS4B protein from hepatitis C virus (HCV) is a highly hydrophobic protein inducing a rearrangement of endoplasmic reticulum membranes responsible of the HCV replication process. Different helical elements have been found in the N- and C- terminal domains of the protein, which seem to be...read more

Mentioned in this Paper

Tissue Membrane
Carboxy-Terminal Amino Acid
Viral Nonstructural Proteins NS2
Hepatitis C
Plasma Protein Binding Capacity
Membrane Activity
Infrared Spectrophotometry
Anisotropy
Polypeptides
Calorimetry, Differential Scanning
Paper Details
References
  • References44
  • Citations10
12345
  • References44
  • Citations10
1

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Membrane interaction of segment H1 (NS4B(H1)) from hepatitis C virus non-structural protein 4B

Biochimica Et Biophysica Acta

Jan 5, 2011

M Francisca Palomares-Jerez, José Villalaín

PMID: 21195690

DOI: 10.1016/j.bbamem.2010.12.023

Abstract

NS4B protein from hepatitis C virus (HCV) is a highly hydrophobic protein inducing a rearrangement of endoplasmic reticulum membranes responsible of the HCV replication process. Different helical elements have been found in the N- and C- terminal domains of the protein, which seem to be...read more

Mentioned in this Paper

Tissue Membrane
Carboxy-Terminal Amino Acid
Viral Nonstructural Proteins NS2
Hepatitis C
Plasma Protein Binding Capacity
Membrane Activity
Infrared Spectrophotometry
Anisotropy
Polypeptides
Calorimetry, Differential Scanning

Similar Papers Found In These Feeds

Hepatitis C

Hepatitis C virus causes acute and chronic liver disease in humans, including chronic hepatitis, cirrhosis, and hepatocellular carcinoma. Discover the latest research on Hepatitis C here.

Related Papers

Biochimica Et Biophysica Acta

Interaction with membranes of the full C-terminal domain of protein NS4B from hepatitis C virus

Biochimica Et Biophysica ActaJuly 4, 2012
M Francisca Palomares-JerezJosé Villalaín
Paper Details
References
  • References44
  • Citations10
12345
  • References44
  • Citations10
1
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