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

Analysis of the functional significance of amino acid residues in the putative NTP-binding pattern of the poliovirus 2C protein.

The Journal of general virology - 1 Aug 1992

Teterina N L, Kean K M, Gorbalenya A E, Agol V I, Girard M

Abstract excerpt

The amino acid sequence of the poliovirus 2C protein contains two highly conserved stretches, GSPGTGKS136 and MDD177, which correspond to the consensus 'A' and 'B' motifs (GXXXXGKS/T and DD/E, respectively) found in nucleoside triphosphate-binding proteins. To assess the functional importance of these amino acid sequences, we changed conserved and non-conserved amino acids. The replacement of the non-conserved...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Base Sequence

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

Share to Binding Sites

Share to Cloning, Molecular

Share to Escherichia coli

Share to Molecular Sequence Data

Share to Phenotype

Share to Plasmids

Source

Identifiers

PMID: 1322957
DOI: 10.1099/0022-1317-73-8-1977

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

Analysis of the functional significance of amino acid residues in the putative NTP-binding pattern of the poliovirus 2C protein.PMID 1322957Read ↗

Genetic studies on the poliovirus 2C protein, an NTPase. A plausible mechanism of guanidine effect on the 2C function and evidence for the importance of 2C oligomerization.Semantic proximity Read ↗

Alanine scanning of poliovirus 2CATPase reveals new genetic evidence that capsid protein/2CATPase interactions are essential for morphogenesis.Semantic proximity Read ↗

Inefficient complementation activity of poliovirus 2C and 3D proteins for rescue of lethal mutations.Semantic proximity Read ↗

Poliovirus protein 2C contains two regions involved in RNA binding activity.Semantic proximity Read ↗

A C-terminal, cysteine-rich site in poliovirus 2C(ATPase) is required for morphogenesis.Semantic proximity Read ↗

A cysteine-rich motif in poliovirus protein 2C(ATPase) is involved in RNA replication and binds zinc in vitro.Semantic proximity Read ↗

An intragenic revertant of a poliovirus 2C mutant has an uncoating defect.Semantic proximity Read ↗

Evidence for Functional Protein Interactions Required for Poliovirus RNA ReplicationSemantic proximity Read ↗

Three poliovirus 2B mutants exhibit noncomplementable defects in viral RNA amplification and display dosage-dependent dominance over wild-type poliovirus.Semantic proximity Read ↗

A Single Amino Acid Substitution in Poliovirus Nonstructural Protein 2CATPase Causes Conditional Defects in Encapsidation and Uncoating.Semantic proximity Read ↗

Identification of regions of poliovirus 2BC protein that are involved in cytotoxicity.Semantic proximity Read ↗

Substitutions in the protease (3Cpro) gene of poliovirus can suppress a mutation in the 5' noncoding region.Semantic proximity Read ↗

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