Evidence map›Paper›PMID 20072699›Full record

ArticlePloS one2010

Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78.

Magdalena Wisniewska, Tobias Karlberg, Lari Lehtiö, Ida Johansson, Tetyana Kotenyova, Martin Moche, Herwig Schüler

Abstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing 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

86 citing papers in PubMed.

  1. Article
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  7. Review
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  9. Article
  10. The Role of BAG3 Protein Interactions in Cardiomyopathies.International journal of molecular sciences · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. HSPA6 and its role in cancers and other diseases.Molecular biology reports · 2022
    Review
  17. Article
  18. Article
  19. Article
  20. Article

26 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

7 authors.

Magdalena WisniewskaStructural Genomics Consortium, Karolinska Institutet, Stockholm, Sweden.
Tobias Karlberg
Lari Lehtiö
Ida Johansson
Tetyana Kotenyova
Martin Moche
Herwig Schüler

Funding

CIHRWellcome Trust
6 · The paper itself

Abstract

unlabelledThe 70-kDa heat shock proteins (Hsp70) are chaperones with central roles in processes that involve polypeptide remodeling events. Hsp70 proteins consist of two major functional domains: an N-terminal nucleotide binding domain (NBD) with ATPase activity, and a C-terminal substrate binding domain (SBD). We present the first crystal structures of four human Hsp70 isoforms, those of the NBDs of HSPA1L, HSPA2, HSPA5 and HSPA6. As previously with Hsp70 family members, all four proteins crystallized in a closed cleft conformation, although a slight cleft opening through rotation of subdomain IIB was observed for the HSPA5-ADP complex. The structures presented here support the view that the NBDs of human Hsp70 function by conserved mechanisms and contribute little to isoform specificity, which instead is brought about by the SBDs and by accessory proteins. ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceCrystallography, X-RayDNA, ComplementaryEndoplasmic Reticulum Chaperone BiPHSP70 Heat-Shock ProteinsHumansModels, MolecularMolecular Sequence DataProtein ConformationProtein IsoformsSequence Homology, Amino AcidAdenosine TriphosphatasesDNA, ComplementaryEndoplasmic Reticulum Chaperone BiPHSP70 Heat-Shock ProteinsHSPA5 protein, humanProtein Isoforms

Identifiers

PMID20072699
PMCPMC2803158

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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.