Evidence map›Paper›PMID 23812373›Full record

ArticleNature structural & molecular biology2013

Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle.

Zhuo Li, F Ulrich Hartl, Andreas Bracher

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

49 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. Article
  3. Mechanisms and regulation of the Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2026
    Review
  4. Recent insights into HSP70: proteostasis and beyond.Frontiers in molecular biosciences · 2026
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Viruses Hijack ERAD to Regulate Their Replication and Propagation.International journal of molecular sciences · 2022
    Review
  13. Article
  14. Review
  15. Review
  16. Review
  17. The STI1-domain is a flexible alpha-helical fold with a hydrophobic groove.Protein science : a publication of the Protein Society · 2021
    Article
  18. Article
  19. Review
  20. Article
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.

Zhuo LiDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.
F Ulrich Hartl
Andreas Bracher
Max Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Hsp70-interacting protein, Hip, cooperates with the chaperone Hsp70 in protein folding and prevention of aggregation. Hsp70 interacts with non-native protein substrates in an ATP-dependent reaction cycle regulated by J-domain proteins and nucleotide exchange factors (NEFs). Hip is thought to delay substrate release by slowing ADP dissociation from Hsp70. Here we present crystal structures of the dimerization domain and the tetratricopeptide repeat (TPR) domain of rat Hip. As shown in a cocrystal structure, the TPR core of Hip interacts with the Hsp70 ATPase domain through an extensive interface, to form a bracket that locks ADP in the binding cleft. Hip and NEF binding to Hsp70 are mutually exclusive, and thus Hip attenuates active cycling of Hsp70-substrate complexes. This mechanism explains how Hip enhances aggregation prevention by Hsp70 and facilitates transfer of specific proteins to downstream chaperones or the proteasome.

Indexed as

Models, MolecularProtein ConformationAdenosine DiphosphateAnimalsbeta-GalactosidaseCalorimetryCarrier ProteinsChromatography, GelCloning, MolecularCrystallizationDimerizationEscherichia coliHSP70 Heat-Shock ProteinsKineticsMolecular Chaperonesortho-AminobenzoatesAdenosine Diphosphatebeta-GalactosidaseCarrier ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesN(8)-(4-((N'-methylanthraniloyl)amino)butyl)-8-aminoadenosine 5'-diphosphateortho-AminobenzoatesSt13 protein, ratTumor Suppressor Proteins

Identifiers

PMID23812373
OpenAlexW2004384163

What OpenQuestion holds

Textmetadata
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.