Evidence map›Paper›PMID 20735087›Full record

ArticleBiochemistry2010

Direct evidence of conformational heterogeneity in human pancreatic glucokinase from high-resolution nuclear magnetic resonance.

Mioara Larion, Roberto K Salinas, Lei Bruschweiler-Li, Rafael Brüschweiler, Brian G Miller

Abstract read
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.9field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function.Progress in nuclear magnetic resonance spectroscopy · 2016
    Review
  8. Dual allosteric activation mechanisms in monomeric human glucokinase.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  9. Article
  10. Article
  11. Role of connecting loop I in catalysis and allosteric regulation of human glucokinase.Protein science : a publication of the Protein Society · 2014
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Homotropic allosteric regulation in monomeric mammalian glucokinase.Archives of biochemistry and biophysics · 2012
    Review
  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

5 authors at 2 institutions in 1 country.

Mioara LarionDepartment of Chemistry and Biochemistry, The Florida State University, Tallahassee, Florida 32306-4390, USA.
Roberto K Salinas
Lei Bruschweiler-Li
Rafael Brüschweiler
Brian G Miller
Florida State University · USNational High Magnetic Field Laboratory · US

Funding

Human GlucokinaseR01DK081358 · NIDDK · FLORIDA STATE UNIVERSITY · PI MILLER, BRIAN GENE · 2009 to 2013
$1.4M
NIDDK NIH HHS 1R01DK081358NIDDK NIH HHS R01 DK081358
6 · The paper itself

Abstract

High-resolution nuclear magnetic resonance is used to investigate the conformational dynamics of human glucokinase, a 52 kDa monomeric enzyme that displays kinetic cooperativity. (1)H-(15)N transverse relaxation optimized spectra of uniformly labeled glucokinase, recorded in the absence and presence of glucose, reveal significant cross-peak overlap and heterogeneous peak intensities that persist over a range of temperatures. (15)N-specific labeling of isoleucines and tryptophans, reporting on backbone and side chain dynamics, respectively, demonstrates that both unliganded and glucose-bound enzymes sample multiple conformations, although glucose stabilizes certain conformations. These results provide the first direct evidence of glucokinase conformational heterogeneity and hence shed light on the molecular basis of cooperativity.

Indexed as

GlucokinaseGlucoseHumansMagnetic Resonance ImagingMolecular ConformationPancreasGlucokinaseGlucose

Identifiers

PMID20735087
PMCPMC3023983
OpenAlexW2074755045

What OpenQuestion holds

Textmetadata
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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.