Evidence map›Paper›PMID 38327055›Full record

ArticleBiophysical journal2024

pH-dependent reaction triggering in PmHMGR crystals for time-resolved crystallography.

Vatsal Purohit, Calvin N Steussy, Anthony R Rosales, Chandra J Critchelow, Tim Schmidt, Paul Helquist, Olaf Wiest, Andrew Mesecar, Aina E Cohen, Cynthia V Stauffacher

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. 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

10 authors.

Vatsal PurohitDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana.
Calvin N SteussyDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana.
Anthony R RosalesDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana.
Chandra J CritchelowDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana.
Tim SchmidtDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana.
Paul HelquistDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana.
Olaf WiestDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana.
Andrew MesecarDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana; Purdue Institute for Cancer Research, Purdue University, West Lafayette, Indiana; Department of Biochemistry, Purdue University, West Lafayette, Indiana.
Aina E CohenStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California.
Cynthia V StauffacherDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana; Purdue Institute of Inflammation, Immunology and Infectious Diseases, Purdue University, West Lafayette, Indiana; Purdue Institute for Cancer Research, Purdue University, West Lafayette, Indiana. Electronic address: cstauffa@purdue.edu.

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI Andrea L Kasinski · 1985 to 2026
$43.4M
A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Ritimukta Sarangi · 2020 to 2026
$43.3M
Chemistry-Biochemistry-Biology Training Program at Notre DameT32GM075762 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CHANG, MAYLAND F, MOBASHERY, SHAHRIAR · 2007 to 2021
$3.7M
Determination of structure, dynamics and energetics of enzyme reactionsR01GM111645 · NIGMS · UNIVERSITY OF NOTRE DAME · PI WIEST, OLAF G · 2015 to 2023
$2.5M
High-Speed High-Sensitivity Detector for X-ray Micro-Crystallography at GM/CA@APSS10OD012289 · OD · UNIVERSITY OF CHICAGO · PI FISCHETTI, ROBERT F. · 2014 to 2014
$2.0M
NCI NIH HHS P30 CA023168NIGMS NIH HHS P30 GM133894NIGMS NIH HHS R01 GM111645NIGMS NIH HHS T32 GM075762NIH HHS S10 OD012289
6 · The paper itself

Abstract

Serial crystallography and time-resolved data collection can readily be employed to investigate the catalytic mechanism of Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl (HMG)-coenzyme-A (CoA) reductase (PmHMGR) by changing the environmental conditions in the crystal and so manipulating the reaction rate. This enzyme uses a complex mechanism to convert mevalonate to HMG-CoA using the co-substrate CoA and cofactor NAD

Indexed as

Hydroxymethylglutaryl CoA ReductasesNADCrystallographyHydrogen-Ion ConcentrationKineticsMevalonic AcidHydroxymethylglutaryl CoA ReductasesMevalonic AcidNAD

Identifiers

PMID38327055
PMCPMC10938121

What OpenQuestion holds

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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.