Evidence map›Paper›PMID 28708998›Full record

ArticleCell2017

Profiling Ssb-Nascent Chain Interactions Reveals Principles of Hsp70-Assisted Folding.

Kristina Döring, Nabeel Ahmed, Trine Riemer, Harsha Garadi Suresh, Yevhen Vainshtein, Markus Habich, Jan Riemer, Matthias P Mayer, Edward P O'Brien, Günter Kramer and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed, 1 pooled it
9.3field-weighted citation impact, top 1% 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

103 citing papers in PubMed, 1 synthesis or guideline pooled it, 201 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. More than the 'master regulator of cytosolic proteostasis': new roles for HSF1 in promoting tissue health.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Functions of J-domain proteins in mitochondrial protein biogenesis.Protein science : a publication of the Protein Society · 2026
    Review
  12. Article
  13. Mitochondrial presequences are more than just address labels.Protein science : a publication of the Protein Society · 2026
    Review
  14. Review
  15. Article
  16. Article
  17. Cotranslational assembly directs the biogenesis of the mProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  18. Article
  19. Article
  20. Review

43 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

11 authors at 4 institutions in 3 countries.

Kristina DöringCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg, Germany; German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, Heidelberg, Germany.
Nabeel AhmedBioinformatics and Genomics Graduate Program, The Huck Institutes of the Life Sciences, Pennsylvania State University, University Park, PA, USA.
Trine RiemerCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg, Germany; German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, Heidelberg, Germany.
Harsha Garadi SureshCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg, Germany; German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, Heidelberg, Germany; The Donnelly Centre, University of Toronto, 160 College Street, Toronto ON, Canada.
Yevhen VainshteinCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg, Germany.
Markus HabichInstitute of Biochemistry, University of Cologne, Zuelpicher Str. 47, Cologne, Germany.
Jan RiemerInstitute of Biochemistry, University of Cologne, Zuelpicher Str. 47, Cologne, Germany.
Matthias P MayerCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg, Germany.
Edward P O'BrienBioinformatics and Genomics Graduate Program, The Huck Institutes of the Life Sciences, Pennsylvania State University, University Park, PA, USA; Department of Chemistry, Pennsylvania State University, University Park, PA, USA.
Günter KramerCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg, Germany; German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, Heidelberg, Germany. Electronic address: g.kramer@zmbh.uni-heidelberg.de.
Bernd BukauCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg, Germany; German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, Heidelberg, Germany. Electronic address: bukau@zmbh.uni-heidelberg.de.
DKFZ-ZMBH Alliance · DEHeidelberg University · DEPennsylvania State University · USUniversity of Cologne · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast Hsp70 chaperone Ssb interacts with ribosomes and nascent polypeptides to assist protein folding. To reveal its working principle, we determined the nascent chain-binding pattern of Ssb at near-residue resolution by in vivo selective ribosome profiling. Ssb associates broadly with cytosolic, nuclear, and hitherto unknown substrate classes of mitochondrial and endoplasmic reticulum (ER) nascent proteins, supporting its general chaperone function. Ssb engages most substrates by multiple binding-release cycles to a degenerate sequence enriched in positively charged and aromatic amino acids. Timely association with this motif upon emergence at the ribosomal tunnel exit requires ribosome-associated complex (RAC) but not nascent polypeptide-associated complex (NAC). Ribosome footprint densities along orfs reveal faster translation at times of Ssb binding, mainly imposed by biases in mRNA secondary structure, codon usage, and Ssb action. Ssb thus employs substrate-tailored dynamic nascent chain associations to coordinate co-translational protein folding, facilitate accelerated translation, and support membrane targeting of organellar proteins.

Indexed as

Protein FoldingAdenosine TriphosphatasesAmino Acid MotifsHSP70 Heat-Shock ProteinsModels, MolecularProtein BiosynthesisRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesHSP70 Heat-Shock ProteinsSaccharomyces cerevisiae ProteinsSSB1 protein, S cerevisiaeSSB2 protein, S cerevisiaechaperoneco-translational foldingHsp70NACRAACSelective ribosome profilingSsbtranslation

Identifiers

PMID28708998
PMCPMC7343536
OpenAlexW2736142726

What OpenQuestion holds

Textmetadata
LicenceTDM
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.