Evidence map›Paper›PMID 26245978›Full record

ArticleNature communications2015

Multiple cellular proteins interact with LEDGF/p75 through a conserved unstructured consensus motif.

Petr Tesina, Kateřina Čermáková, Magdalena Hořejší, Kateřina Procházková, Milan Fábry, Subhalakshmi Sharma, Frauke Christ, Jonas Demeulemeester, Zeger Debyser, Jan De Rijck and 2 more

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In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed, 1 pooled it
2.9field-weighted citation impact, top 9% 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

44 citing papers in PubMed, 1 synthesis or guideline pooled it, 73 citations in OpenAlex.

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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

12 authors at 4 institutions in 2 countries.

Petr TesinaInstitute of Organic Chemistry and Biochemistry of the ASCR, v.v.i., Flemingovo nam. 2, 166 10 Prague, Czech Republic.
Kateřina ČermákováKU Leuven, Molecular Virology and Gene Therapy, Kapucijnenvoer 33, B-3000 Leuven, Belgium.
Magdalena HořejšíInstitute of Molecular Genetics of the ASCR, v.v.i., Videnska 1083, 142 20 Prague, Czech Republic.
Kateřina ProcházkováInstitute of Organic Chemistry and Biochemistry of the ASCR, v.v.i., Flemingovo nam. 2, 166 10 Prague, Czech Republic.
Milan FábryInstitute of Molecular Genetics of the ASCR, v.v.i., Videnska 1083, 142 20 Prague, Czech Republic.
Subhalakshmi SharmaKU Leuven, Molecular Virology and Gene Therapy, Kapucijnenvoer 33, B-3000 Leuven, Belgium.
Frauke ChristKU Leuven, Molecular Virology and Gene Therapy, Kapucijnenvoer 33, B-3000 Leuven, Belgium.
Jonas DemeulemeesterKU Leuven, Molecular Virology and Gene Therapy, Kapucijnenvoer 33, B-3000 Leuven, Belgium.
Zeger DebyserKU Leuven, Molecular Virology and Gene Therapy, Kapucijnenvoer 33, B-3000 Leuven, Belgium.
Jan De RijckKU Leuven, Molecular Virology and Gene Therapy, Kapucijnenvoer 33, B-3000 Leuven, Belgium.
Václav VeverkaInstitute of Organic Chemistry and Biochemistry of the ASCR, v.v.i., Flemingovo nam. 2, 166 10 Prague, Czech Republic.
Pavlína ŘezáčováInstitute of Organic Chemistry and Biochemistry of the ASCR, v.v.i., Flemingovo nam. 2, 166 10 Prague, Czech Republic.
KU Leuven · BECzech Academy of Sciences, Institute of Molecular Genetics · CZCzech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZCharles University · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lens epithelium-derived growth factor (LEDGF/p75) is an epigenetic reader and attractive therapeutic target involved in HIV integration and the development of mixed lineage leukaemia (MLL1) fusion-driven leukaemia. Besides HIV integrase and the MLL1-menin complex, LEDGF/p75 interacts with various cellular proteins via its integrase binding domain (IBD). Here we present structural characterization of IBD interactions with transcriptional repressor JPO2 and domesticated transposase PogZ, and show that the PogZ interaction is nearly identical to the interaction of LEDGF/p75 with MLL1. The interaction with the IBD is maintained by an intrinsically disordered IBD-binding motif (IBM) common to all known cellular partners of LEDGF/p75. In addition, based on IBM conservation, we identify and validate IWS1 as a novel LEDGF/p75 interaction partner. Our results also reveal how HIV integrase efficiently displaces cellular binding partners from LEDGF/p75. Finally, the similar binding modes of LEDGF/p75 interaction partners represent a new challenge for the development of selective interaction inhibitors.

Indexed as

Amino Acid SequenceCell Cycle ProteinsConsensus SequenceDimerizationDNA-Binding ProteinsEscherichia coliHistone-Lysine N-MethyltransferaseHIV IntegraseHumansIntercellular Signaling Peptides and ProteinsLentivirusMolecular Sequence DataMyeloid-Lymphoid Leukemia ProteinProteinsProtein Structure, TertiaryRepressor ProteinsCDCA7L protein, humanCell Cycle ProteinsDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseHIV IntegraseIntercellular Signaling Peptides and ProteinsIws1 protein, humanKMT2A protein, humanlens epithelium-derived growth factorMyeloid-Lymphoid Leukemia ProteinPOGZ protein, humanProteinsRepressor ProteinsRNA-Binding ProteinsTranscription FactorsTransposases

Identifiers

PMID26245978
OpenAlexW1863439705

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.