Evidence map›Paper›PMID 34747601›Full record

ArticleBiochemistry2021

Structure, Function, and Thermodynamics of Lactate Dehydrogenases from Humans and the Malaria Parasite

Sergei Khrapunov, Akiba Waterman, Rudra Persaud, Eric P Chang

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Biochemical characteristics of patients with imported malaria.Frontiers in cellular and infection microbiology · 2022
    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

4 authors at 2 institutions in 1 country.

Sergei KhrapunovDepartment of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, United States.ORCID 0000-0002-6181-9525
Akiba WatermanDepartment of Chemistry and Physical Sciences, Pace University, 1 Pace Plaza, New York, New York 10038, United States.
Rudra PersaudDepartment of Chemistry and Physical Sciences, Pace University, 1 Pace Plaza, New York, New York 10038, United States.
Eric P ChangDepartment of Chemistry and Physical Sciences, Pace University, 1 Pace Plaza, New York, New York 10038, United States.
Pace University · 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
NIGMS NIH HHS P01 GM068036
6 · The paper itself

Abstract

Temperature adaptation is ubiquitous among all living organisms, yet the molecular basis for this process remains poorly understood. It can be assumed that for parasite-host systems, the same enzymes found in both organisms respond to the same selection factor (human body temperature) with similar structural changes. Herein, we report the existence of a reversible temperature-dependent structural transition for the glycolytic enzyme lactate dehydrogenase (LDH) from the malaria parasite

Indexed as

AcclimatizationAntimalarialsBody TemperatureHot TemperatureHumansLactate DehydrogenasesMalaria, FalciparumMyocardiumPlasmodium falciparumProtozoan ProteinsSequence AlignmentSpecies SpecificityStructure-Activity RelationshipSubstrate SpecificityThermodynamicsAntimalarialsLactate DehydrogenasesProtozoan Proteins

Identifiers

PMID34747601
PMCPMC8672703
OpenAlexW3211661410

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.