Evidence map›Paper›PMID 42731393›Full record

ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2026

NMR relaxation dispersion reveals an order of magnitude range of acid loop motions in protein tyrosine phosphatase 1B.

Ryan M Anderson, J Patrick Loria

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Ryan M AndersonDepartment of Chemistry, Yale University, New Haven, CT 06511, United States.
J Patrick LoriaDepartment of Chemistry, Yale University, New Haven, CT 06511, United States; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, United States. Electronic address: patrick.loria@yale.edu.

Funding

PREDOCTORAL PROGRAM IN BIOPHYSICST32GM008283 · NIGMS · YALE UNIVERSITY · PI XIONG, YONG · 1988 to 2022
$10.5M
Mechanism of catalytic regulation and active site loop motions in related protein tyrosine phosphatasesR01GM112781 · NIGMS · YALE UNIVERSITY · PI LORIA, JOSEPH P · 2015 to 2024
$2.8M
Predoctoral Program in BiophysicsT32GM149438 · NIGMS · YALE UNIVERSITY · PI Yong Xiong, Elsa Chui Ying Yan · 2023 to 2026
$2.6M
NIGMS NIH HHS R01 GM112781NIGMS NIH HHS T32 GM008283NIGMS NIH HHS T32 GM149438
6 · The paper itself

Abstract

Motion of the active site acid loop is critical for the proper function of the enzyme, protein tyrosine phosphatase 1B (PTP1B). To investigate the motion of this loop, we incorporated 7-fluorotryptophan at residue 179 (7F-Trp) near the hinge of the acid loop - replacing the naturally occurring tryptophan at this position. Control experiments show identical k

Indexed as

(19)F NMRCPMG relaxation dispersionLoop dynamicsProtein tyrosine phosphatasePTP1BR(1ρ) relaxation dispersion

Identifiers

PMID42731393
PMCPMC13636088

What OpenQuestion holds

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Registered trials

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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.