Evidence map›Paper›PMID 28696262›Full record

ArticleThe Journal of biological chemistry2017

Human serine racemase structure/activity relationship studies provide mechanistic insight and point to position 84 as a hot spot for β-elimination function.

David L Nelson, Greg A Applegate, Matthew L Beio, Danielle L Graham, David B Berkowitz

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2017. 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
1.4field-weighted citation impact, top 21% 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

14 citing papers in PubMed, 26 citations in OpenAlex.

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  4. Information-Rich, Dual-FunctionJournal of the American Chemical Society · 2023
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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

5 authors at 1 institution in 1 country.

David L NelsonFrom the Department of Chemistry, University of Nebraska, Lincoln, Nebraska 68588.
Greg A ApplegateFrom the Department of Chemistry, University of Nebraska, Lincoln, Nebraska 68588.
Matthew L BeioFrom the Department of Chemistry, University of Nebraska, Lincoln, Nebraska 68588.
Danielle L GrahamFrom the Department of Chemistry, University of Nebraska, Lincoln, Nebraska 68588.
David B BerkowitzFrom the Department of Chemistry, University of Nebraska, Lincoln, Nebraska 68588. Electronic address: dberkowitz1@unl.edu.
University of Nebraska–Lincoln · US

Funding

EXTRAMURAL RES FACILITIES CONSTRC06RR016544 · NCRR · UNIVERSITY OF NEBRASKA LINCOLN · PI PAUL, PREM S · 2001 to 2001
$2.0M
NCRR NIH HHS C06 RR016544
6 · The paper itself

Abstract

There is currently great interest in human serine racemase, the enzyme responsible for producing the NMDA co-agonist d-serine. Reported correlation of d-serine levels with disorders including Alzheimer's disease, ALS, and ischemic brain damage (elevated d-serine) and schizophrenia (reduced d-serine) has further piqued this interest. Reported here is a structure/activity relationship study of position Ser

Indexed as

Models, MolecularAmino Acid SubstitutionArginineBinding, CompetitiveBiocatalysisComputational BiologyEnzyme InhibitorsHumansHydrogen BondingKineticsMolecular Docking SimulationMolecular Dynamics SimulationMutationPDZ DomainsPeptide FragmentsPhylogenyArginineEnzyme InhibitorsPeptide FragmentsRacemases and EpimerasesRecombinant Fusion ProteinsRecombinant ProteinsSerineSerine Racemaseenzyme kineticsenzyme mechanismmolecular modelingpyridoxal phosphatesite-directed mutagenesis

Identifiers

PMID28696262
PMCPMC5572919
OpenAlexW2735736903

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.