Evidence map›Paper›PMID 25701377›Full record

ReviewProgress in biophysics and molecular biology2015

Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif.

Qian Wu, Harry Jubb, Tom L Blundell

Abstract readReview
In one paragraph

Review in Progress in biophysics and molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

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  7. ACS omega · 2022
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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

3 authors.

Qian WuDepartment of Biochemistry, 80 Tennis Court Road, University of Cambridge, CB2 1GA, Cambridge, United Kingdom. Electronic address: qw222@cam.ac.uk.
Harry JubbDepartment of Biochemistry, 80 Tennis Court Road, University of Cambridge, CB2 1GA, Cambridge, United Kingdom.
Tom L BlundellDepartment of Biochemistry, 80 Tennis Court Road, University of Cambridge, CB2 1GA, Cambridge, United Kingdom.

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust 093167/Z/10/Z
6 · The paper itself

Abstract

BRCA1 BRCT domains function as phosphoprotein-binding modules for recognition of the phosphorylated protein-sequence motif pSXXF. While the motif interaction interface provides strong anchor points for binding, protein regions outside the motif have recently been found to be important for binding affinity. In this review, we compare the available structural data for BRCA1 BRCT domains in complex with phosphopeptides in order to gain a more complete understanding of the interaction between phosphopeptides and BRCA1-BRCT domains.

Indexed as

Models, ChemicalModels, MolecularAmino Acid MotifsAmino Acid SequenceBinding SitesBRCA1 ProteinComputer SimulationDNA DamageDNA RepairMolecular Sequence DataPhosphopeptidesProtein BindingProtein ConformationProtein Structure, TertiaryBRCA1 ProteinPhosphopeptidesBRCA1BRCTDNA damage responsePhosphopeptidepSXXF motifTandem BRCT domains

Identifiers

PMID25701377
PMCPMC4728184

What OpenQuestion holds

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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.