Evidence map›Paper›PMID 30565457›Full record

ArticleBiochemistry2019

Probing the Electrostatic and Steric Requirements for Substrate Binding in Human Platelet-Type 12-Lipoxygenase.

Ansari Mukhtar Aleem, Wan-Chen Tsai, Jennyfer Tena, Gabriella Alvarez, Joshua Deschamps, Chakrapani Kalyanaraman, Matthew P Jacobson, Theodore Holman

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Biochemistry · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. A 12-lipoxygenase-Gpr31 signaling axis is required for pancreatic organogenesis in the zebrafish.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  12. Review
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

8 authors at 2 institutions in 1 country.

Ansari Mukhtar AleemDepartment of Chemistry and Biochemistry , University of California Santa Cruz , Santa Cruz , California 95064 , United States.
Wan-Chen TsaiDepartment of Chemistry and Biochemistry , University of California Santa Cruz , Santa Cruz , California 95064 , United States.
Jennyfer TenaDepartment of Chemistry and Biochemistry , University of California Santa Cruz , Santa Cruz , California 95064 , United States.
Gabriella Alvarez
Joshua DeschampsDepartment of Chemistry and Biochemistry , University of California Santa Cruz , Santa Cruz , California 95064 , United States.
Chakrapani KalyanaramanDepartment of Pharmaceutical Chemistry, School of Pharmacy , University of California San Francisco , San Francisco , California 94143 , United States.
Matthew P JacobsonDepartment of Pharmaceutical Chemistry, School of Pharmacy , University of California San Francisco , San Francisco , California 94143 , United States.ORCID 0000-0001-6262-655X
Theodore HolmanDepartment of Chemistry and Biochemistry , University of California Santa Cruz , Santa Cruz , California 95064 , United States.ORCID 0000-0001-8072-2959
University of California, Santa Cruz · USUniversity of California, San Francisco · US

Funding

UCSC PREPR25GM104552 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI William T. SULLIVAN · 2013 to 2026
$3.9M
Discovery of Potent 12-Lipoxygenase Inhibitors of Platelet ActivationR01AG047986 · NIA · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI HOLMAN, THEODORE R · 2014 to 2016
$1.4M
NIA NIH HHS R01 AG047986NIGMS NIH HHS R25 GM104552
6 · The paper itself

Abstract

Human platelet ALOX12 (hALOX12 or h12-LOX) has been implicated in a variety of human diseases. The present study investigates the active site of hALOX12 to more thoroughly understand how it positions the substrate and achieves nearly perfect regio- and stereospecificities (i.e., 100 ± 5% of the 12(S)-hydroperoxide product), utilizing site-directed mutagenesis. Specifically, we have determined that Arg402 is not as important in substrate binding as previously seen for hALOX15 but that His596 may play a role in anchoring the carboxy terminal of the arachidonic acid during catalysis. In addition, Phe414 creates a π-stacking interaction with a double bond of arachidonic acid (Δ

Indexed as

Arachidonate 12-LipoxygenaseArachidonic AcidBlood PlateletsCatalysisCatalytic DomainHumansKineticsMolecular Docking SimulationMutagenesis, Site-DirectedMutationProtein BindingStatic ElectricitySubstrate SpecificityALOX12 protein, humanArachidonate 12-LipoxygenaseArachidonic Acid

Identifiers

PMID30565457
PMCPMC7270147
OpenAlexW2903810113

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.