Evidence map›Paper›PMID 23259601›Full record

ReviewACS chemical biology2013

Transition States, analogues, and drug development.

Vern L Schramm

Abstract readReview
In one paragraph

Review in ACS chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

53 citing papers in PubMed, 151 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Capturing the free energy of transition state stabilization: insights from the inhibition of mandelate racemase.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

1 author at 1 institution in 1 country.

Vern L SchrammDepartment of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx New York 10461, United States. vern.schramm@einstein.yu.edu
Albert 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
Purine Pathways and Inhibitor Design in PlasmodiumR01AI049512 · NIAID · YESHIVA UNIVERSITY · PI SCHRAMM, VERN L. · 2002 to 2012
$4.8M
RICIN--MECHANISM, TRANSITION STATE AND INHIBITOR DESIGNR01CA072444 · NCI · YESHIVA UNIVERSITY · PI SCHRAMM, VERN L. · 1997 to 2011
$4.4M
TRANSITION STATE ANALYSIS OF ENZYMATIC REACTIONSR37GM041916 · NIGMS · YESHIVA UNIVERSITY · PI SCHRAMM, VERN L. · 1998 to 2007
$3.5M
Transition State Analogues as Modulators of DNA MethylationR01CA135405 · NCI · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI SCHRAMM, VERN L. · 2008 to 2018
$2.8M
NCI NIH HHS CA072444NCI NIH HHS CA135405NCI NIH HHS R01 CA072444NCI NIH HHS R01 CA135405NIAID NIH HHS AI049512NIAID NIH HHS R01 AI049512NIGMS NIH HHS GM068036NIGMS NIH HHS GM41916NIGMS NIH HHS P01 GM068036NIGMS NIH HHS R01 GM041916NIGMS NIH HHS R37 GM041916
6 · The paper itself

Abstract

Enzymes achieve their transition states by dynamic conformational searches on the femtosecond to picosecond time scale. Mimics of reactants at enzymatic transition states bind tightly to enzymes by stabilizing the conformation optimized through evolution for transition state formation. Instead of forming the transient transition state geometry, transition state analogues convert the short-lived transition state to a stable thermodynamic state. Enzymatic transition states are understood by combining kinetic isotope effects and computational chemistry. Analogues of the transition state can bind millions of times more tightly than substrates and show promise for drug development for several targets.

Indexed as

Drug DesignModels, BiologicalEnzymesHIV ProteaseHIV Protease InhibitorsIndinavirKineticsModels, MolecularEnzymesHIV ProteaseHIV Protease InhibitorsIndinavir

Identifiers

PMID23259601
PMCPMC3560411
OpenAlexW2084257914

What OpenQuestion holds

Textmetadata
LicenceTDM
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.