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

The NS5A protein of hepatitis C virus is a zinc metalloprotein.

The Journal of biological chemistry - 19 Nov 2004

Tellinghuisen Timothy L, Marcotrigiano Joseph, Gorbalenya Alexander E, Rice Charles M

Abstract excerpt

The NS5A protein of hepatitis C virus is believed to be an integral part of the viral replicase. Despite extensive investigation, the role of this protein remains elusive. Only limited biochemical characterization of NS5A has been performed, with most research to date involving the myriad of host proteins and signaling cascades that interact with NS5A. The need for better characterization of NS5A is paramount for...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Cysteine
Share to Electroporation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Metalloproteins

Share to Spectrophotometry, Atomic

Share to Trypsin

Share to Viral Nonstructural Proteins

Source

Identifiers

PMID: 15339921
DOI: 10.1074/jbc.M407787200

Provenance

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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The NS5A protein of hepatitis C virus is a zinc metalloprotein.PMID 15339921Read ↗

Structural and functional insights into alphavirus polyprotein processing and pathogenesis.Semantic proximity Read ↗

Host and Viral Zinc-Finger Proteins in COVID-19Semantic proximity Read ↗

Dodecamer Structure of Severe Acute Respiratory Syndrome Coronavirus Nonstructural Protein nsp10Semantic proximity Read ↗

Strict Conservation of the Retroviral Nucleocapsid Protein Zinc Finger Is Strongly Influenced by Its Role in Viral Infection Processes: Characterization of HIV-1 Particles Containing Mutant Nucleocapsid Zinc-Coordinating SequencesSemantic proximity Read ↗

What a twist: structural biology of the SARS-CoV-2 helicase nsp13Semantic proximity Read ↗

Structural features stabilized by divalent cation coordination within hepatitis E virus ORF1 are critical for viral replicationSemantic proximity Read ↗

Structure Prediction and Analysis of Hepatitis E Virus Non-Structural Proteins from the Replication and Transcription Machinery by AlphaFold2Semantic proximity Read ↗

Ebola virus transcription activator VP30 is a zinc-binding protein.Semantic proximity Read ↗

The intrinsic disorder status of the human hepatitis C virus proteome.Semantic proximity Read ↗

Zinc fingers--the next antiviral target?Semantic proximity Read ↗

X-ray Structural and Functional Studies of the Three Tandemly Linked Domains of Non-structural Protein 3 (nsp3) from Murine Hepatitis Virus Reveal Conserved FunctionsSemantic proximity Read ↗

The nsp15 Nuclease as a Good Target to Combat SARS-CoV-2: Mechanism of Action and Its Inactivation with FDA-Approved DrugsSemantic proximity Read ↗

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