Evidence map›Paper›PMID 20095049›Full record

ArticleProtein science : a publication of the Protein Society2010

Structural basis for unfolding pathway-dependent stability of proteins: vectorial unfolding versus global unfolding.

Keisuke Yagawa, Koji Yamano, Takaomi Oguro, Masahiro Maeda, Takehiro Sato, Takaki Momose, Shin Kawano, Toshiya Endo

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

13 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Folding pathway of an Ig domain is conserved on and off the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  7. Article
  8. Article
  9. Article
  10. Mimicking Ribosomal Unfolding of RNA Pseudoknot in a Protein Channel.Journal of the American Chemical Society · 2015
    Article
  11. Structure of giant muscle proteins.Frontiers in physiology · 2013
    Review
  12. Conformational stability of CopC and roles of residues Tyr79 and Trp83.Protein science : a publication of the Protein Society · 2013
    Article
  13. 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

8 authors at 1 institution in 1 country.

Keisuke YagawaDepartment of Chemistry, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.
Koji Yamano
Takaomi Oguro
Masahiro Maeda
Takehiro Sato
Takaki Momose
Shin Kawano
Toshiya Endo
Nagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Point mutations in proteins can have different effects on protein stability depending on the mechanism of unfolding. In the most interesting case of I27, the Ig-like module of the muscle protein titin, one point mutation (Y9P) yields opposite effects on protein stability during denaturant-induced "global unfolding" versus "vectorial unfolding" by mechanical pulling force or cellular unfolding systems. Here, we assessed the reason for the different effects of the Y9P mutation of I27 on the overall molecular stability and N-terminal unraveling by NMR. We found that the Y9P mutation causes a conformational change that is transmitted through beta-sheet structures to reach the central hydrophobic core in the interior and alters its accessibility to bulk solvent, which leads to destabilization of the hydrophobic core. On the other hand, the Y9P mutation causes a bend in the backbone structure, which leads to the formation of a more stable N-terminal structure probably through enhanced hydrophobic interactions.

Indexed as

Protein ConformationCircular DichroismConnectinKineticsMicroscopy, Atomic ForceMitochondriaModels, MolecularMuscle ProteinsMutationNuclear Magnetic Resonance, BiomolecularProtein FoldingProtein KinasesProteinsProtein StabilityThermodynamicsConnectinMuscle ProteinsProtein KinasesProteins

Identifiers

PMID20095049
PMCPMC2867010
OpenAlexW2134483008

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.