Evidence map›Paper›PMID 29915028›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Inverse enzyme isotope effects in human purine nucleoside phosphorylase with heavy asparagine labels.

Rajesh K Harijan, Ioanna Zoi, Dimitri Antoniou, Steven D Schwartz, Vern L Schramm

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Transitioning enzyme catalysis towards photocatalysis.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Inverse heavy enzyme isotope effects in methylthioadenosine nucleosidases.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
  12. Role of Protein Motions in Catalysis by Formate Dehydrogenase.The journal of physical chemistry. B · 2020
    Article
  13. Article
  14. Heavy Enzymes and the Rational Redesign of Protein Catalysts.Chembiochem : a European journal of chemical biology · 2019
    Article
  15. Modification of Enzyme Activity by Vibrational Strong Coupling of Water.Angewandte Chemie (International ed. in English) · 2019
    Article
  16. Article
  17. 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

5 authors at 2 institutions in 1 country.

Rajesh K HarijanDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461.
Ioanna ZoiDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721.
Dimitri AntoniouDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721.
Steven D SchwartzDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721 vern.schramm@einstein.yu.edu sschwartz@email.arizona.edu.
Vern L SchrammDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461; vern.schramm@einstein.yu.edu sschwartz@email.arizona.edu.
University of Arizona · USAlbert Einstein College of Medicine · US

Funding

Proton Transfer Dynamics in Heme-Copper OxidasesP01GM068036 · NIGMS · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI CALLENDER, ROBERT · 2004 to 2018
$26.4M
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 P01 GM068036NIGMS NIH HHS R01 GM041916NIGMS NIH HHS R37 GM041916
6 · The paper itself

Abstract

Transition path-sampling calculations with several enzymes have indicated that local catalytic site femtosecond motions are linked to transition state barrier crossing. Experimentally, femtosecond motions can be perturbed by labeling the protein with amino acids containing

Indexed as

AsparagineCatalysisHumansIsotope LabelingIsotopesKineticsPurine-Nucleoside PhosphorylaseAsparagineIsotopesPurine-Nucleoside PhosphorylaseBorn–Oppenheimer enzymesheavy-enzyme isotope effectspromoting vibrationstransition path samplingtransition state structure

Identifiers

PMID29915028
PMCPMC6142206
OpenAlexW2809028771

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.