Cargando…
A eukaryotic cytosolic chaperonin is associated with a high molecular weight intermediate in the assembly of hepatitis B virus capsid, a multimeric particle
We have established a system for assembly of hepatitis B virus capsid, a homomultimer of the viral core polypeptide, using cell-free transcription-linked translation. The mature particles that are produced are indistinguishable from authentic viral capsids by four criteria: velocity sedimentation, b...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1994
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2120005/ https://www.ncbi.nlm.nih.gov/pubmed/7908022 |
Ejemplares similares
-
The Cytosolic Chaperonin CCT/TRiC and Cancer Cell Proliferation
por: Boudiaf-Benmammar, Chafika, et al.
Publicado: (2013) -
Single-Ring Intermediates Are Essential for Some Chaperonins
por: Bhatt, Jay M., et al.
Publicado: (2018) -
Looking for Novel Capsid Protein Multimerization Inhibitors of Feline Immunodeficiency Virus
por: Sierra, Natalia, et al.
Publicado: (2018) -
Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT
por: Booth, Christopher R, et al.
Publicado: (2008) -
Mechanistic insights into protein folding by the eukaryotic chaperonin complex CCT
por: Smith, Theresa M., et al.
Publicado: (2022)