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Article

Hepatitis C virus core protein: carboxy-terminal boundaries of two processed species suggest cleavage by a signal peptide peptidase.

Virology - 1 Oct 1996

Hüssy P, Langen H, Mous J, Jacobsen H

Abstract excerpt

The expression and processing of hepatitis C virus core protein was analyzed. Two protein bands, 21 kDa (P21), corresponding to the full-length core, and 19 kDa (P19), were detected as major products when core protein was expressed in the standard rabbit reticulocyte lysate system or in Sf9 insect cells. Core proteins with amino-terminal hexa-histidine tags were expressed which allowed the purification of the...

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Source

Identifiers

PMID: 8862403
DOI: 10.1006/viro.1996.0510

Genes

DHFR

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Hepatitis C virus core protein: carboxy-terminal boundaries of two processed species suggest cleavage by a signal peptide peptidase.PMID 8862403Read ↗

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Identification of basic amino acids at the N-terminal end of the core protein that are crucial for hepatitis C virus infectivity.Semantic proximity Read ↗

Processing in the hepatitis C virus E2-NS2 region: identification of p7 and two distinct E2-specific products with different C terminiSemantic proximity Read ↗

Intramembrane processing by signal peptide peptidase regulates the membrane localization of hepatitis C virus core protein and viral propagation.Semantic proximity Read ↗

The arginine-rich domain of hepatitis B virus precore and core proteins contains a signal for nuclear transportSemantic proximity Read ↗

Core protein cleavage by signal peptide peptidase is required for hepatitis C virus-like particle assembly.Semantic proximity Read ↗

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Characterization of hepatitis C virus core protein multimerization and membrane envelopment: revelation of a cascade of core-membrane interactions.Semantic proximity Read ↗

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