Evidence map›Paper›PMID 29152711›Full record

ArticleBiopolymers2018

The burst-phase folding intermediate of ribonuclease H changes conformation over evolutionary history.

Shion A Lim, Susan Marqusee

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biopolymers, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Evolution of the folding landscape of effector caspases.The Journal of biological chemistry · 2021
    Article
  4. Evolution, folding, and design of TIM barrels and related proteins.Current opinion in structural biology · 2021
    Review
  5. 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

2 authors.

Shion A LimDepartment of Molecular and Cell Biology, University of California, Berkeley, California.
Susan MarquseeDepartment of Molecular and Cell Biology, University of California, Berkeley, California.ORCID http://orcid.org/0000-0003-2136-2732

Funding

Sequence and Environmental Determinants of the Protein Energy LandscapeR01GM050945 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI MARQUSEE, SUSAN · 1999 to 2022
$7.4M
FOLDING OF THE ACID STATE, SUBDOMAINS AND INTACT RNASE HR29GM050945 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI MARQUSEE, SUSAN · 1994 to 1998
–
National Institute of General Medical Sciences GM050945NIGMS NIH HHS R01 GM050945
6 · The paper itself

Abstract

The amino acid sequence encodes the energy landscape of a protein. Therefore, we expect evolutionary mutations to change features of the protein energy landscape, including the conformations adopted by a polypeptide as it folds to its native state. Ribonucleases H (RNase H) from Escherichia coli and Thermus thermophilus both fold via a partially folded intermediate in which the core region of the protein (helices A-D and strands 4-5) is structured. Strand 1, however, uniquely contributes to the T. thermophilus RNase H folding intermediate (I

Indexed as

Evolution, MolecularProtein FoldingEscherichia coliEscherichia coli ProteinsProtein DomainsRibonuclease HThermus thermophilusEscherichia coli ProteinsRibonuclease Hancestral sequence reconstructionenergy landscapefolding intermediatesprotein evolutionprotein folding

Identifiers

PMID29152711
PMCPMC6047922

What OpenQuestion holds

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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.