Evidence map›Paper›PMID 35294247›Full record

ArticleScience advances2022

Assembly mechanism of early Hsp90-Cdc37-kinase complexes.

Dimitra Keramisanou, M V Vasantha Kumar, Nicole Boose, Rinat R Abzalimov, Ioannis Gelis

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 29 citations in OpenAlex.

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  16. BRAFScience advances · 2023
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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

5 authors at 2 institutions in 1 country.

Dimitra KeramisanouDepartment of Chemistry, University of South Florida, Tampa, FL 33620, USA.ORCID 0000-0003-2677-3063
M V Vasantha KumarDepartment of Chemistry, University of South Florida, Tampa, FL 33620, USA.
Nicole BooseDepartment of Chemistry, University of South Florida, Tampa, FL 33620, USA.ORCID 0000-0001-6966-9595
Rinat R AbzalimovStructural Biology Initiative, CUNY Advanced Science Research Center, New York, NY 10031, USA.ORCID 0000-0003-2110-1532
Ioannis GelisDepartment of Chemistry, University of South Florida, Tampa, FL 33620, USA.ORCID 0000-0001-8099-003X
University of South Florida · USThe Graduate Center, CUNY · US

Funding

Assembly mechanism of cochaperone-kinase complexesR01GM115854 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI GELIS, IOANNIS · 2015 to 2019
$1.6M
NIGMS NIH HHS R01 GM115854
6 · The paper itself

Abstract

Molecular chaperones have an essential role for the maintenance of a balanced protein homeostasis. Here, we investigate how protein kinases are recruited and loaded to the Hsp90-Cdc37 complex, the first step during Hsp90-mediated chaperoning that leads to enhanced client kinase stability and activation. We show that conformational dynamics of all partners is a critical feature of the underlying loading mechanism. The kinome co-chaperone Cdc37 exists primarily in a dynamic extended conformation but samples a low-populated, well-defined compact structure. Exchange between these two states is maintained in an assembled Hsp90-Cdc37 complex and is necessary for substrate loading. Breathing motions at the N-lobe of a free kinase domain partially expose the kinase segment trapped in the Hsp90 dimer downstream in the cycle. Thus, client dynamics poise for chaperone dependence. Hsp90 is not directly involved during loading, and Cdc37 is assigned the task of sensing clients by stabilizing the preexisting partially unfolded client state.

Identifiers

PMID35294247
PMCPMC8926337
OpenAlexW4221012102

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.