Evidence map›Paper›PMID 8861969›Full record

ArticleThe EMBO journal1996

A conserved domain of the large subunit of replication factor C binds PCNA and acts like a dominant negative inhibitor of DNA replication in mammalian cells.

R Fotedar, R Mossi, P Fitzgerald, T Rousselle, G Maga, H Brickner, H Messier, S Kasibhatla, U Hübscher, A Fotedar

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.8field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Mechanism of opening a sliding clamp.Nucleic acids research · 2017
    Article
  6. Review
  7. Replication clamps and clamp loaders.Cold Spring Harbor perspectives in biology · 2013
    Review
  8. Article
  9. Review
  10. BRCT domains: easy as one, two, three.Cell cycle (Georgetown, Tex.) · 2011
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

R FotedarInstitut de Biologie Structurale J.-P. Ebel, Grenoble, France.
R Mossi
P Fitzgerald
T Rousselle
G Maga
H Brickner
H Messier
S Kasibhatla
U Hübscher
A Fotedar
Université Grenoble Alpes · FRInstitut de Biologie Structurale · FR

Funding

NOVEL POU PROTEIN AND LYMPHOCYTE GENE EXPRESSIONR01AI031453 · NIAID · SIDNEY KIMMEL CANCER CENTER · PI FOTEDAR, ARUN · 1995 to 1999
–
NIAID NIH HHS AI31453-01
6 · The paper itself

Abstract

Replication factor C (RF-C), a complex of five polypeptides, is essential for cell-free SV40 origin-dependent DNA replication and viability in yeast. The cDNA encoding the large subunit of human RF-C (RF-Cp145) was cloned in a Southwestern screen. Using deletion mutants of RF-Cp145 we have mapped the DNA binding domain of RF-Cp145 to amino acid residues 369-480. This domain is conserved among both prokaryotic DNA ligases and eukaryotic poly(ADP-ribose) polymerases and is absent in other subunits of RF-C. The PCNA binding domain maps to amino acid residues 481-728 and is conserved in all five subunits of RF-C. The PCNA binding domain of RF-Cp145 inhibits several functions of RF-C, such as: (i) in vitro DNA replication of SV40 origin-containing DNA; (ii) RF-C-dependent loading of PCNA onto DNA; and (iii) RF-C-dependent DNA elongation. The PCNA binding domain of RF-Cp145 localizes to the nucleus and inhibits DNA synthesis in transfected mammalian cells. In contrast, the DNA binding domain of RF-Cp145 does not inhibit DNA synthesis in vitro or in vivo. We therefore conclude that amino acid residues 481-728 of human RF-Cp145 are critical and act as a dominant negative mutant of RF-C function in DNA replication in vivo.

Indexed as

Homeodomain ProteinsProto-Oncogene Proteins c-bcl-2Repressor ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceDepression, ChemicalDNA-Binding ProteinsDNA, ComplementaryDNA ReplicationHumansLeukemia-Lymphoma, Adult T-CellMacromolecular SubstancesMinor Histocompatibility AntigensMolecular Sequence DataPeptide FragmentsProliferating Cell Nuclear AntigenBCL2-related protein A1DNA-Binding ProteinsDNA, ComplementaryHomeodomain ProteinsMacromolecular SubstancesMATA1 protein, S cerevisiaeMinor Histocompatibility AntigensPeptide FragmentsProliferating Cell Nuclear AntigenProto-Oncogene Proteins c-bcl-2Recombinant Fusion ProteinsReplication Protein CRepressor ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID8861969
PMCPMC452166
OpenAlexW302805760

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.