Evidence map›Paper›PMID 28495594›Full record

ArticleJournal of structural biology2017

Elevated μs-ms timescale backbone dynamics in the transition state analog form of arginine kinase.

Omar Davulcu, Yu Peng, Rafael Brüschweiler, Jack J Skalicky, Michael S Chapman

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of structural biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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.

Omar DavulcuDepartment of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97239, United States.
Yu PengDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, United States.
Rafael BrüschweilerDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, United States; Department of Biological Chemistry and Pharmacology and Campus Chemical Instrument Center, The Ohio State University, OH 43210, United States.
Jack J SkalickyDepartment of Biochemistry, University of Utah, Salt Lake City, UT 84112, United States.
Michael S ChapmanDepartment of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97239, United States. Electronic address: chapmami@ohsu.edu.

Funding

Adeno-Associated Virus Gene Therapy Vectors: Molecular Interactions on Cell EntryR35GM122564 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI MICHAEL S. CHAPMAN · 2017 to 2026
$6.7M
Functional Dynamics During Induced-fit Enzyme TurnoverR01GM077643 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI CHAPMAN, MICHAEL S. · 2007 to 2015
$2.7M
NIGMS NIH HHS R01 GM077643NIGMS NIH HHS R35 GM122564
6 · The paper itself

Abstract

Arginine kinase catalyzes reversible phosphoryl transfer between arginine and ATP. Crystal structures of arginine kinase in an open, substrate-free form and closed, transition state analog (TSA) complex indicate that the enzyme undergoes substantial domain and loop rearrangements required for substrate binding, catalysis, and product release. Nuclear magnetic resonance (NMR) has shown that substrate-free arginine kinase is rigid on the ps-ns timescale (average S

Indexed as

Adenosine DiphosphateArginineArginine KinaseHumansModels, MolecularNitratesNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein DomainsAdenosine DiphosphateArginineArginine KinaseNitratesNitrogen IsotopesArginine kinaseDynamicsNMRRelaxation dispersionTransition state analog

Identifiers

PMID28495594
PMCPMC5677571

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.