Evidence map›Paper›PMID 33410323›Full record

ArticleBiochemistry2021

Protein Mass-Modulated Effects in Alkaline Phosphatase.

Ananda K Ghosh, Vern L Schramm

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemistry, 2021. 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

2 authors.

Ananda K GhoshDepartment of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, United States.ORCID 0000-0002-5485-4760
Vern L SchrammDepartment of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, United States.ORCID 0000-0002-8056-1929

Funding

TRANSITION STATE ANALYSIS OF ENZYMATIC REACTIONSR01GM041916 · NIGMS · YESHIVA UNIVERSITY · PI SCHRAMM, VERN L. · 1989 to 2023
$10.0M
TRANSITION STATE ANALYSIS OF ENZYMATIC REACTIONSR37GM041916 · NIGMS · YESHIVA UNIVERSITY · PI SCHRAMM, VERN L. · 1998 to 2007
$3.5M
NIGMS NIH HHS R01 GM041916NIGMS NIH HHS R37 GM041916
6 · The paper itself

Abstract

Recent experimental studies engaging isotopically substituted protein (heavy protein) have revealed that many, but not all, enzymatic systems exhibit altered chemical steps in response to an altered mass. The results have been interpreted as femtosecond protein dynamics at the active site being linked (or not) to transition-state barrier crossing. An altered enzyme mass can influence several kinetic parameters (

Indexed as

Alkaline PhosphataseBinding SitesCatalysisCatalytic DomainEscherichia coliEscherichia coli ProteinsKineticsModels, MolecularProtein ConformationAlkaline PhosphataseEscherichia coli Proteins

Identifiers

PMID33410323
PMCPMC8340299

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.