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

Solution structure of the hRPABC14.4 subunit of human RNA polymerases.

Nature structural biology - 1 Nov 1999

del Río-Portilla F, Gaskell A, Gilbert D, Ladias J A, Wagner G

Abstract excerpt

The protein hRPABC14.4 is an essential subunit of human RNA polymerases I, II, and III and is required for the transcription of all human nuclear genes. The structure of hRPABC14.4 was determined by nuclear magnetic resonance spectroscopy. The protein fold comprises a highly conserved central domain forming two antiparallel alpha-helices flanked by the less conserved N- and C-terminal regions forming a...

Read the complete abstract on PubMed

Topics

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

Share to Conserved Sequence
Share to DNA-Directed RNA Polymerases
Share to Nuclear Magnetic Resonance, Biomolecular

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

Share to Protein Structure, Secondary

Share to Protein Subunits

Share to Solutions

Share to Static Electricity

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 10542096
DOI: 10.1038/14923

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

Solution structure of the hRPABC14.4 subunit of human RNA polymerases.PMID 10542096Read ↗

The intrinsically unstructured domain of PC4 modulates the activity of the structured core through inter- and intramolecular interactions.Semantic proximity Read ↗

The human RNA polymerase I structure reveals an HMG-like transcription factor docking domain specific to metazoansSemantic proximity Read ↗

Structure of human RNA polymerase III.Semantic proximity Read ↗

An evolutionarily conserved tryptophan cage promotes folding of the extended RNA recognition motif in the hnRNPR-like protein familySemantic proximity Read ↗

Cryo-EM structures of human RNA polymerase III in its unbound and transcribing statesSemantic proximity Read ↗

Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1.Semantic proximity Read ↗

Nucleic acid sequence determinants of transcriptional pausing by human mitochondrial RNA polymerase (POLRMT)Semantic proximity Read ↗

Dimer-dimer stacking interactions are important for nucleic acid binding by the archaeal chromatin protein Alba.Semantic proximity Read ↗

Structural insights into human TFIIIC promoter recognitionSemantic proximity Read ↗

Functional architecture of RNA polymerase I.Semantic proximity Read ↗

A key role for the alpha 1 helix of human RAP74 in the initiation and elongation of RNA chains.Semantic proximity Read ↗

The 2.2-Å structure of the HP0958 protein from Helicobacter pylori reveals a kinked anti-parallel coiled-coil hairpin domain and a highly conserved ZN-ribbon domain.Semantic proximity Read ↗

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