Evidence map›Paper›PMID 19519518›Full record

ReviewProtein and peptide letters2009

Heat shock protein 40: structural studies and their functional implications.

Jingzhi Li, Xinguo Qian, Bingdong Sha

Open access · greenAbstract readReview
In one paragraph

Review in Protein and peptide letters, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
2.8field-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

67 citing papers in PubMed, 129 citations in OpenAlex.

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  9. Mitochondrial dysfunction in Alzheimer's disease: Guiding the path to targeted therapies.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
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7 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

Jingzhi LiDepartment of Cell Biology, University of Alabama at Birmingham, AL 35294, USA.
Xinguo Qian
Bingdong Sha
University of Alabama at Birmingham · US

Funding

STRUCTURAL AND FUNCTIONAL STUDIES OF HSP40R01DK056203 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SHA, BINGDONG · 1999 to 2010
$2.7M
Structural and Functional Studies for Mitochondrial Protein TranslocationsR01GM080261 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SHA, BINGDONG · 2007 to 2015
$2.4M
NIDDK NIH HHS R01 DK056203NIGMS NIH HHS R01 GM080261
6 · The paper itself

Abstract

The mechanism by which Hsp40 and other molecular chaperones recognize and interact with non-native polypeptides is a fundamental question, as is how Hsp40 co-operates with Hsp70 to facilitate protein folding. Years of structural studies of Hsp40 from yeast and other species, conducted using X-ray protein crystallography, NMR and small-angle X-ray scattering, have shed light on the mechanisms how Hsp40 functions as a molecular chaperone and how Hsp40-Hsp70 pair promotes protein folding, protein transport and degradation. This review provides a discussion of recent structural studies of Hsp40s and their functional implications.

Indexed as

Crystallography, X-RayHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHumansNuclear Magnetic Resonance, BiomolecularProtein FoldingProtein Structure, TertiaryHSP40 Heat-Shock ProteinsHSP70 Heat-Shock Proteins

Identifiers

PMID19519518
PMCPMC2755554
OpenAlexW1963807823

What OpenQuestion holds

Textmetadata
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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.