Evidence map›Paper›PMID 15888311›Full record

ReviewBioorganic chemistry2005

Experimental observation of thiamin diphosphate-bound intermediates on enzymes and mechanistic information derived from these observations.

Frank Jordan, Natalia S Nemeria

Abstract readReview
In one paragraph

Review in Bioorganic chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

26 citing papers in PubMed, 55 citations in OpenAlex.

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  5. Potent Inhibition ofACS infectious diseases · 2024
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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

2 authors at 1 institution in 1 country.

Frank JordanDepartment of Chemistry, Rutgers University, Newark, NJ 07102, USA.
Natalia S Nemeria
Rutgers, The State University of New Jersey · US

Funding

STRUCTURE AND MECHANISM OF YEAST PYRUVATE DECARBOXYLASER01GM050380 · NIGMS · RUTGERS THE STATE UNIV OF NJ NEWARK · PI JORDAN, FRANK · 1993 to 2013
$3.0M
MECHANISM OF E. COLI PYRUVATE DEHYDROGENASE COMPLEX-E1R01GM062330 · NIGMS · RUTGERS THE STATE UNIV OF NJ NEWARK · PI JORDAN, FRANK · 2001 to 2004
$1.4M
NIGMS NIH HHS GM-50380NIGMS NIH HHS GM-62330NIGMS NIH HHS R01 GM050380
6 · The paper itself

Abstract

Thiamin diphosphate (ThDP), the vitamin B1 coenzyme, is an excellent representative of coenzymes, which carry out electrophilic catalysis by forming a covalent complex with their substrates. The function of ThDP is to greatly increase the acidity of two carbon acids by stabilizing their conjugate bases, the ylide/C2-carbanion of the thiazolium ring and the C2alpha-carbanion (or enamine) once the substrate binds to ThDP. In recent years, several ThDP-bound intermediates on such pathways have been characterized by both solution and solid-state (X-ray) methods. Prominent among these advances are X-ray crystallographic results identifying both oxidative and non-oxidative intermediates, rapid chemical quench followed by NMR detection of a several intermediates which are stable under acidic conditions, and circular dichroism detection of the 1',4'-imino tautomer of ThDP in some of the intermediates. Some of these methods also enable the investigator to determine the rate-limiting step in the complex series of steps.

Indexed as

CoenzymesCrystallography, X-RayEnzymesModels, MolecularMolecular StructureMultienzyme ComplexesSubstrate SpecificityThiamine PyrophosphateCoenzymesEnzymesMultienzyme ComplexesThiamine Pyrophosphate

Identifiers

PMID15888311
PMCPMC4189838
OpenAlexW1978675965

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.