Evidence map›Paper›PMID 34905349›Full record

ArticleACS chemical biology2022

Bryce P Johnson, Vikas Kumar, Erin M Scull, Leonard M Thomas, Christina R Bourne, Shanteri Singh

Abstract read
In one paragraph

Article in ACS chemical biology, 2022. 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
–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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. 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

6 authors.

Bryce P JohnsonDepartment of Chemistry and Biochemistry, University of Oklahoma, Stephenson Life Sciences Research Center, 101 Stephenson Pkwy, Norman, Oklahoma 73019, United States.
Vikas KumarDepartment of Chemistry and Biochemistry, University of Oklahoma, Stephenson Life Sciences Research Center, 101 Stephenson Pkwy, Norman, Oklahoma 73019, United States.
Erin M ScullDepartment of Chemistry and Biochemistry, University of Oklahoma, Stephenson Life Sciences Research Center, 101 Stephenson Pkwy, Norman, Oklahoma 73019, United States.
Leonard M ThomasDepartment of Chemistry and Biochemistry, University of Oklahoma, Stephenson Life Sciences Research Center, 101 Stephenson Pkwy, Norman, Oklahoma 73019, United States.
Christina R BourneDepartment of Chemistry and Biochemistry, University of Oklahoma, Stephenson Life Sciences Research Center, 101 Stephenson Pkwy, Norman, Oklahoma 73019, United States.ORCID 0000-0001-6192-3392
Shanteri SinghDepartment of Chemistry and Biochemistry, University of Oklahoma, Stephenson Life Sciences Research Center, 101 Stephenson Pkwy, Norman, Oklahoma 73019, United States.ORCID 0000-0003-0960-4794

Funding

Structure-Function Studies of MsvR, a Methanogen-Specific Transcriptional RegulaP20GM103640 · NIGMS · UNIVERSITY OF OKLAHOMA · PI THOMAS, LEONARD M · 2012 to 2021
$20.4M
NIGMS NIH HHS P20 GM103640
6 · The paper itself

Abstract

Isopentenyl phosphate kinases (IPKs) catalyze the ATP-dependent phosphorylation of isopentenyl monophosphate (IP) to isopentenyl diphosphate (IPP) in the alternate mevalonate pathways of the archaea and plant cytoplasm. In recent years, IPKs have also been employed in artificial biosynthetic pathways called "(iso) prenol pathways" that utilize promiscuous kinases to sequentially phosphorylate (iso) prenol and generate the isoprenoid precursors IPP and dimethylallyl diphosphate (DMAPP). Furthermore, IPKs have garnered attention for their impressive substrate promiscuity toward non-natural alkyl-monophosphates (alkyl-Ps), which has prompted their utilization as biocatalysts for the generation of novel isoprenoids. However, none of the IPK crystal structures currently available contain non-natural substrates, leaving the roles of active-site residues in substrate promiscuity ambiguous. To address this, we present herein the high-resolution crystal structures of an IPK from

Indexed as

ArchaeaArchaeal ProteinsGene Expression Regulation, ArchaealGene Expression Regulation, EnzymologicGenome, ArchaealModels, MolecularMutationProtein ConformationProtein KinasesSubstrate SpecificityArchaeal ProteinsProtein Kinases

Identifiers

PMID34905349
PMCPMC9745668

What Socratic 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 Socratic graph.