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 structural basis of recognition and removal of cellular mRNA 7-methyl G 'caps' by a viral capsid protein: a unique viral response to host defense.

Journal of molecular recognition : JMR - 1 Jan 2000

Tang Jinghua, Naitow Hisashi, Gardner Nora A, Kolesar Anna, Tang Liang, Wickner Reed B, Johnson John E

Abstract excerpt

The single segment, double-stranded RNA genome of the L-A virus (L-A) of yeast encodes two proteins: the major coat protein Gag (76 kDa) and the Gag-Pol fusion protein (180 kDa). The icosahedral L-A capsid is formed by 120 copies of Gag and has architecture similar to that seen in the reovirus, blue tongue virus and rice dwarf virus inner protein shells. Gag chemically removes the m7GMP caps from host cellular...

Read the complete abstract on PubMed

Topics

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

Share to Capsid
Share to Dinucleoside Phosphates

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

Share to Gene Products, gag

Share to Histidine

Share to Phenylalanine

Share to RNA Caps

Share to RNA, Double-Stranded

Share to RNA Viruses

Source

Identifiers

PMID: 15597333
DOI: 10.1002/jmr.724

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The structural basis of recognition and removal of cellular mRNA 7-methyl G 'caps' by a viral capsid protein: a unique viral response to host defense.PMID 15597333Read ↗

Viral genome-capsid core senses host environments to prime RNA releaseSemantic proximity Read ↗

Cap snatching in yeast L-BC double-stranded RNA totivirus.Semantic proximity Read ↗

Requirement for Host RNA-Silencing Components and the Virus-Silencing Suppressor when Second-Site Mutations Compensate for Structural Defects in the 3' Untranslated Region.Semantic proximity Read ↗

φX174 Genome-Capsid Interactions Influence the Biophysical Properties of the Virion: Evidence for a Scaffolding-Like Function for the Genome during the Final Stages of MorphogenesisSemantic proximity Read ↗

Complementary Mutations in the N and L Proteins for Restoration of Viral RNA Synthesis.Semantic proximity Read ↗

Adeno-associated virus capsid proteins may play a role in transcription and second-strand synthesis of recombinant genomes.Semantic proximity Read ↗

Functional analysis of RNA binding by the hepatitis C virus RNA-dependent RNA polymerase.Semantic proximity Read ↗

The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA.Semantic proximity Read ↗

Multiple capsid protein binding sites mediate selective packaging of the alphavirus genomic RNASemantic proximity Read ↗

Crystal structure of vaccinia virus mRNA capping enzyme provides insights into the mechanism and evolution of the capping apparatus.Semantic proximity Read ↗

Cystoviral polymerase complex protein P7 uses its acidic C-terminal tail to regulate the RNA-directed RNA polymerase P2.Semantic proximity Read ↗

Dissecting human cytomegalovirus gene function and capsid maturation by ribozyme targeting and electron cryomicroscopySemantic proximity Read ↗

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