Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Cleavage of vimentin by different retroviral proteases.

Archives of biochemistry and biophysics - 15 May 2000

Snásel J, Shoeman R, Horejsí M, Hrusková-Heidingsfeldová O, Sedlácek J, Ruml T, Pichová I

Abstract excerpt

Proteases (PRs) of retroviruses cleave viral polyproteins into their mature structural proteins and replication enzymes. Besides this essential role in the replication cycle of retroviruses, PRs also cleave a variety of host cell proteins. We have analyzed the in vitro cleavage of mouse vimentin by proteases of human immunodeficiency virus type 1 (HIV-1) and type 2 (HIV-2), bovine leukemia virus (BLV),...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aspartic Acid Endopeptidases
Share to Endopeptidases
Share to HIV Protease

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen-Ion Concentration

Share to Leukemia Virus, Bovine

Share to Retroviridae

Share to Sodium Chloride

Share to Vimentin

Source

Identifiers

PMID: 10845700
DOI: 10.1006/abbi.2000.1776

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cleavage of vimentin by different retroviral proteases.PMID 10845700Read ↗

Retroviral proteases.Semantic proximity Read ↗

Structural and biochemical studies of retroviral proteasesSemantic proximity Read ↗

Biochemical Characterization of Human Retroviral-Like Aspartic Protease 1 (ASPRV1).Semantic proximity Read ↗

Proteolytic processing of foamy virus Gag and Pol proteins.Semantic proximity Read ↗

Matrix Metalloproteinase Activity in Infections by an Encephalitic Virus, Mouse Adenovirus Type 1Semantic proximity Read ↗

Proteolytic activity of novel human immunodeficiency virus type 1 proteinase proteins from a precursor with a blocking mutation at the N terminus of the PR domain.Semantic proximity Read ↗

Avian sarcoma leukemia virus protease linked to the adjacent Gag polyprotein is enzymatically active.Semantic proximity Read ↗

Soluble expression and enzymatic activity evaluation of protease from reticuloendotheliosis virus.Semantic proximity Read ↗

Active foamy virus proteinase is essential for virus infectivity but not for formation of a Pol polyproteinSemantic proximity Read ↗

Polyprotein processing: cis and trans proteolytic activities of Sesbania mosaic virus serine protease.Semantic proximity Read ↗

Reverse transcriptase and protease activities of avian leukosis virus Gag-Pol fusion proteins expressed in insect cells.Semantic proximity Read ↗

Role of the avian retroviral protease in the activation of reverse transcriptase during virion assembly.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.