Evidence map›Paper›PMID 27613871›Full record

ArticleThe Journal of biological chemistry2016

Substrate and Cofactor Dynamics on Guanosine Monophosphate Reductase Probed by High Resolution Field Cycling 31P NMR Relaxometry.

Masha M Rosenberg, Alfred G Redfield, Mary F Roberts, Lizbeth Hedstrom

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.5field-weighted citation impact, top 30% 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

6 citing papers in PubMed, 8 citations in OpenAlex.

  1. High-Resolution Relaxometry for Fragment Screening.Journal of medicinal chemistry · 2026
    Article
  2. Article
  3. High ResolutionFrontiers in molecular biosciences · 2022
    Review
  4. Article
  5. Article
  6. 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 at 2 institutions in 1 country.

Masha M RosenbergFrom the Departments of Biology.
Alfred G RedfieldBiochemistry, and.
Mary F Robertsthe Department of Chemistry, Boston College, Chestnut Hill, Massachusetts 02467-3860 mary.roberts@bc.edu.
Lizbeth HedstromFrom the Departments of Biology, hedstrom@brandeis.edu.ORCID 0000-0001-8432-3322
Boston College · USBrandeis University · US

Funding

XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 1985 to 2011
$17.6M
INOSINE MONOPHOSPHATE DEHYDROGENASER01GM054403 · NIGMS · BRANDEIS UNIVERSITY · PI HEDSTROM, LIZBETH K. · 1998 to 2016
$4.2M
NCRR NIH HHS P41 RR001081NIGMS NIH HHS R01 GM054403
6 · The paper itself

Abstract

Guanosine-5'-monophosphate reductase (GMPR) catalyzes the reduction of GMP to IMP and ammonia with concomitant oxidation of NADPH. Here we investigated the structure and dynamics of enzyme-bound substrates and cofactors by measuring

Indexed as

BiocatalysisCoenzymesCrystallography, X-RayEscherichia coliEscherichia coli ProteinsGMP ReductaseGuanine NucleotidesInosine MonophosphateKineticsMagnetic Resonance SpectroscopyNADPProtein BindingCoenzymesEscherichia coli ProteinsGMP ReductaseGuanine NucleotidesInosine MonophosphateNADPbiophysicscofactor dynamicsdehydrogenaseenzyme catalysisGMPRnuclear magnetic resonance (NMR)nucleoside/nucleotide biosynthesis

Identifiers

PMID27613871
PMCPMC5087720
OpenAlexW2517500983

What OpenQuestion holds

Textmetadata
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.