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

Interaction of the cauliflower mosaic virus coat protein with the pregenomic RNA leader.

Journal of virology - 1 Mar 2000

Guerra-Peraza O, de Tapia M, Hohn T, Hemmings-Mieszczak M

Abstract excerpt

Using the yeast three-hybrid system, the interaction of the Cauliflower mosaic virus (CaMV) pregenomic 35S RNA (pgRNA) leader with the viral coat protein, its precursor, and a series of derivatives was studied. The purine-rich domain in the center of the pgRNA leader was found to specifically interact with the coat protein. The zinc finger motif of the coat protein and the preceding basic domain were essential...

Read the complete abstract on PubMed

Topics

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

Share to 5' Untranslated Regions
Share to Capsid
Share to Caulimovirus

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

Share to Nucleic Acid Conformation

Share to Nucleic Acid Hybridization

Share to Open Reading Frames

Share to Yeasts

Share to Zinc Fingers

Source

Open in PubMed Open full text

Identifiers

PMID: 10666236
DOI: 10.1128/jvi.74.5.2067-2072.2000
PMCID: PMC111687

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

Interaction of the cauliflower mosaic virus coat protein with the pregenomic RNA leader.PMID 10666236Read ↗

Deletions in the conserved amino-terminal basic arm of cucumber mosaic virus coat protein disrupt virion assembly but do not abolish infectivity and cell-to-cell movement.Semantic proximity Read ↗

Massive production of small RNAs from a non-coding region of Cauliflower mosaic virus in plant defense and viral counter-defense.Semantic proximity Read ↗

Replication of Alfamo- and Ilarviruses: Role of the Coat ProteinSemantic proximity Read ↗

Functional analysis of deletion mutants of cucumber mosaic virus RNA3 using an in vitro transcription system.Semantic proximity Read ↗

Evidence for the role of basic amino acids in the coat protein arm region of Cucumber necrosis virus in particle assembly and selective encapsidation of viral RNA.Semantic proximity Read ↗

Degenerate in vitro genetic selection reveals mutations that diminish alfalfa mosaic virus RNA replication without affecting coat protein binding.Semantic proximity Read ↗

Mutations in the alpha-helical region of the amino terminus of the Maize rayado fino virus capsid protein and CP:RNA ratios affect virus-like particle encapsidation of RNAs.Semantic proximity Read ↗

Genetic dissection of the multiple functions of alfalfa mosaic virus coat protein in viral RNA replication, encapsidation, and movement.Semantic proximity Read ↗

Forced evolution reveals the importance of short open reading frame A and secondary structure in the cauliflower mosaic virus 35S RNA leader.Semantic proximity Read ↗

Interaction between cauliflower mosaic virus inclusion body protein and capsid protein: implications for viral assembly.Semantic proximity Read ↗

N-terminal basic amino acids of alfalfa mosaic virus coat protein involved in the initiation of infection.Semantic proximity Read ↗

Deletion of repeated sequences from tobacco mosaic virus mutants with two coat protein genes.Semantic proximity Read ↗

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