Evidence map›Paper›PMID 21776971›Full record

ArticleBiochemistry2011

Native-state interconversion of a metamorphic protein requires global unfolding.

Robert C Tyler, Nathan J Murray, Francis C Peterson, Brian F Volkman

Abstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Article
  2. Article
  3. The conformational landscape of fold-switcher KaiB is tuned to the circadian rhythm timescale.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Fluid protein fold space and its implications.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  6. Review
  7. Heterodimers Are an Integral Component of Chemokine Signaling Repertoire.International journal of molecular sciences · 2023
    Review
  8. Distinguishing features of fold-switching proteins.Protein science : a publication of the Protein Society · 2023
    Review
  9. Reversible switching between two common protein folds in a designed system using only temperature.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. Design and discovery of metamorphic proteins.Current opinion in structural biology · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Bifurcated Hydrogen Bonds and the Fold Switching of Lymphotactin.The journal of physical chemistry. B · 2020
    Article
  17. Article
  18. Review
  19. Article
  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

4 authors.

Robert C TylerDepartment of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA.
Nathan J Murray
Francis C Peterson
Brian F Volkman

Funding

Structural Basis for Chemokine FunctionR01AI058072 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI VOLKMAN, BRIAN F · 2004 to 2019
$4.1M
Structural Basis for Chemokine FunctionR37AI058072 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI Brian F Volkman · 2020 to 2026
$2.8M
Conformational duality in the human chemokine Ltn/XCL1R01AI063325 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI VOLKMAN, BRIAN F · 2005 to 2009
$1.4M
Conformational duality in the human chemokine Ltn/XCL1R56AI063325 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI VOLKMAN, BRIAN F · 2011 to 2011
$352k
NIAID NIH HHS AI058072NIAID NIH HHS AI063325NIAID NIH HHS R01 AI058072NIAID NIH HHS R01 AI063325NIAID NIH HHS R37 AI058072NIAID NIH HHS R56 AI063325
6 · The paper itself

Abstract

Lymphotactin (Ltn) is a unique chemokine that under physiological solution conditions displays large-scale structural heterogeneity, defining a new category of "metamorphic proteins". Previous Ltn studies have indicated that each form is required for proper function, but the mechanism of interconversion remains unknown. Here we have investigated the temperature dependence of kinetic rates associated with interconversion and unfolding by stopped-flow fluorescence to determine transition-state free energies. Comparisons of derived thermodynamic parameters revealed striking similarities between interconversion and protein unfolding. We conclude that Ltn native-state rearrangement proceeds by way of a large-scale unfolding process rather than a unique intermediate structure.

Indexed as

Protein UnfoldingChemokines, CHumansKineticsModels, MolecularProtein ConformationTemperatureThermodynamicsChemokines, CXCL1 protein, human

Identifiers

PMID21776971
PMCPMC3160782

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.