Evidence map›Paper›PMID 9285825›Full record

ArticleMolecular biology of the cell1997

Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells.

D K Eggers, W J Welch, W J Hansen

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

41 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Dual Leucine Zipper Kinase Regulates Dscam Expression through a Noncanonical Function of the Cytoplasmic Poly(A)-Binding Protein.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
  5. Article
  6. Role of Hsp90 in Plasmodium falciparum Malaria.Advances in experimental medicine and biology · 2021
    Article
  7. General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021
    Article
  8. Article
  9. Ribopuromycylation in Coronavirus-Infected Cells.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
  10. Review
  11. Article
  12. Article
  13. A Plant Biologist's Toolbox to Study Translation.Frontiers in plant science · 2018
    Review
  14. Review
  15. Protein Translation Activity: A New Measure of Host Immune Cell Activation.Journal of immunology (Baltimore, Md. : 1950) · 2016
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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.

D K EggersDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, USA.
W J Welch
W J Hansen
University of California, San Francisco · US

Funding

STRUCTURE/FUNCTION OF THE STRESS PROTEINSR01GM033551 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI WELCH, WILLIAM J · 1985 to 2004
$1.6M
NIGMS NIH HHS 5 R01 GM33551
6 · The paper itself

Abstract

Folding of newly synthesized proteins in vivo is believed to be facilitated by the cooperative interaction of a defined group of proteins known as molecular chaperones. We investigated the direct interaction of chaperones with nascent polypeptides in the cytosol of mammalian cells by multiple methods. A new approach using a polyclonal antibody to puromycin allowed us to tag and capture a population of truncated nascent polypeptides with no bias as to the identity of the bound chaperones. In addition, antibodies that recognize the cytosolic chaperones hsp70, CCT (TRiC), hsp40, p48 (Hip), and hsp90 were compared on the basis of their ability to coprecipitate nascent polypeptides, both before and after chemical cross-linking. By all three approaches, hsp70 was found to be the predominant chaperone bound to nascent polypeptides. The interaction between hsp70 and nascent polypeptides is apparently dynamic under physiological conditions but can be stabilized by depletion of ATP or by cross-linking. The cytosolic chaperonin CCT was found to bind primarily to full-length, newly synthesized actin, and tubulin. We demonstrate and caution that nascent polypeptides have a propensity for binding many proteins nonspecifically in cell lysates. Although current models of protein folding in vivo have described additional components in contact with nascent polypeptides, our data indicate that the hsp70 and, perhaps, the hsp90 families are the predominant classes of molecular chaperones that interact with the general population of cytosolic nascent polypeptides.

Indexed as

Anti-Bacterial AgentsElectrophoresis, Polyacrylamide GelEndopeptidasesHeLa CellsHSP70 Heat-Shock ProteinsHumansMolecular ChaperonesPeptidesPrecipitin TestsPuromycinSensitivity and SpecificityAnti-Bacterial AgentsEndopeptidasesHSP70 Heat-Shock ProteinsMolecular ChaperonesPeptidesPuromycin

Identifiers

PMID9285825
PMCPMC276176
OpenAlexW2165057293

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.