Evidence map›Paper›PMID 27502157›Full record

ArticleJournal of the American Chemical Society2016

Evolution of a Protein Interaction Domain Family by Tuning Conformational Flexibility.

Dustin S Whitney, Brian F Volkman, Kenneth E Prehoda

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Metamorphic protein folding as evolutionary adaptation.Trends in biochemical sciences · 2023
    Review
  6. Article
  7. Article
  8. Harnessing Conformational Plasticity to Generate Designer Enzymes.Journal of the American Chemical Society · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

3 authors.

Dustin S WhitneyDepartment of Biochemistry, Medical College of Wisconsin , Milwaukee, Wisconsin 53226, United States.
Brian F VolkmanDepartment of Biochemistry, Medical College of Wisconsin , Milwaukee, Wisconsin 53226, United States.
Kenneth E PrehodaDepartment of Chemistry and Biochemistry, Institute of Molecular Biology, University of Oregon , Eugene, Oregon 97403, United States.

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
Regulated spindle orientation during asymmetric cell divisionR01GM087457 · NIGMS · UNIVERSITY OF OREGON · PI PREHODA, KENNETH E · 2010 to 2013
$1.3M
NIAID NIH HHS R01 AI058072NIAID NIH HHS R37 AI058072NIGMS NIH HHS R01 GM087457
6 · The paper itself

Abstract

Conformational flexibility allows proteins to adopt multiple functionally important conformations but can also lead to nonfunctional structures. We analyzed the dynamic behavior of the enzyme guanylate kinase as it evolved into the GK protein interaction domain (GK

Indexed as

Molecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularProtein Interaction Domains and MotifsGuanylate KinasesProtein ConformationGuanylate Kinases

Identifiers

PMID27502157
PMCPMC5661941

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.