Evidence map›Paper›PMID 28875036›Full record

ArticleIUCrJ2017

Active-site protein dynamics and solvent accessibility in native

Kakali Sen, Sam Horrell, Demet Kekilli, Chin W Yong, Thomas W Keal, Hakan Atakisi, David W Moreau, Robert E Thorne, Michael A Hough, Richard W Strange

Open access · goldAbstract read
In one paragraph

Article in IUCrJ, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

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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

10 authors at 3 institutions in 2 countries.

Kakali SenSchool of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, England.
Sam HorrellSchool of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, England.
Demet KekilliSchool of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, England.
Chin W YongScientific Computing Department, STFC Daresbury Laboratory, Warrington WA4 4AD, England.ORCID https://orcid.org/0000-0002-6346-7383
Thomas W KealScientific Computing Department, STFC Daresbury Laboratory, Warrington WA4 4AD, England.ORCID https://orcid.org/0000-0001-8747-3975
Hakan AtakisiPhysics Department, Cornell University, Ithaca, NY 14853, USA.
David W MoreauPhysics Department, Cornell University, Ithaca, NY 14853, USA.
Robert E ThornePhysics Department, Cornell University, Ithaca, NY 14853, USA.
Michael A HoughSchool of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, England.ORCID https://orcid.org/0000-0001-7377-6713
Richard W StrangeSchool of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, England.ORCID https://orcid.org/0000-0001-8825-3608
University of Essex · GBCornell University · USDaresbury Laboratory · GB

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
TRAINING IN MOLECULAR PHYSICS OF BIOLOGICAL SYSTEMST32GM008267 · NIGMS · CORNELL UNIVERSITY ITHACA · PI WANG, MICHELLE D. · 1988 to 2021
$9.6M
NIGMS NIH HHS P41 GM103485NIGMS NIH HHS T32 GM008267
6 · The paper itself

Abstract

Microbial nitrite reductases are denitrifying enzymes that are a major component of the global nitrogen cycle. Multiple structures measured from one crystal (MSOX data) of copper nitrite reductase at 240 K, together with molecular-dynamics simulations, have revealed protein dynamics at the type 2 copper site that are significant for its catalytic properties and for the entry and exit of solvent or ligands to and from the active site. Molecular-dynamics simulations were performed using different protonation states of the key catalytic residues (Asp

Indexed as

catalysiscopper nitrite reductasedenitrificationdensity functional theoryhigh temperaturemolecular dynamicsradiolysisserial crystallographysynchrotron radiation

Identifiers

PMID28875036
PMCPMC5571812
OpenAlexW2624763121

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.