Evidence map›Paper›PMID 32125828›Full record

ArticleBiochemistry2020

Protein Farnesyltransferase Catalyzes Unanticipated Farnesylation and Geranylgeranylation of Shortened Target Sequences.

Sudhat Ashok, Emily R Hildebrandt, Colby S Ruiz, Daniel S Hardgrove, David W Coreno, Walter K Schmidt, James L Hougland

Abstract read
In one paragraph

Article in Biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Review
  2. Prelamin A in anArteriosclerosis, thrombosis, and vascular biology · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Comprehensive analysis of CXXX sequence space reveals thatbioRxiv : the preprint server for biology · 2024
    Article
  13. Review
  14. Article
  15. Article
  16. Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023
    Review
  17. Article
  18. Review
  19. Review
  20. 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

7 authors.

Sudhat AshokDepartment of Chemistry, Syracuse University, Syracuse, New York 13244, United States.
Emily R HildebrandtDepartment of Biochemistry & Molecular Biology, University of Georgia, Athens, Georgia 30602, United States.
Colby S RuizDepartment of Biochemistry & Molecular Biology, University of Georgia, Athens, Georgia 30602, United States.
Daniel S HardgroveDepartment of Biochemistry & Molecular Biology, University of Georgia, Athens, Georgia 30602, United States.
David W CorenoDepartment of Chemistry, Syracuse University, Syracuse, New York 13244, United States.
Walter K SchmidtDepartment of Biochemistry & Molecular Biology, University of Georgia, Athens, Georgia 30602, United States.
James L HouglandDepartment of Chemistry, Syracuse University, Syracuse, New York 13244, United States.ORCID 0000-0003-0444-1017

Funding

Determining the scope of prenylatable protein sequencesR01GM132606 · NIGMS · UNIVERSITY OF GEORGIA · PI KANNAN, NATARAJAN, SCHMIDT, WALTER K · 2019 to 2022
$1.6M
Role of Proteolysis in Regulating CaaX Protein FunctionR01GM117148 · NIGMS · UNIVERSITY OF GEORGIA · PI SCHMIDT, WALTER K · 2016 to 2019
$1.2M
NIGMS NIH HHS R01 GM117148NIGMS NIH HHS R01 GM132606
6 · The paper itself

Abstract

Protein prenylation is a posttranslational modification involving the attachment of a C15 or C20 isoprenoid group to a cysteine residue near the C-terminus of the target substrate by protein farnesyltransferase (FTase) or protein geranylgeranyltransferase type I (GGTase-I), respectively. Both of these protein prenyltransferases recognize a C-terminal "CaaX" sequence in their protein substrates, but recent studies in yeast- and mammalian-based systems have demonstrated FTase can also accept sequences that diverge in length from the canonical four-amino acid motif, such as the recently reported five-amino acid C(x)

Indexed as

Amino Acid MotifsFarnesyltranstransferaseKineticsPrenylationProtein PrenylationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityFarnesyltranstransferaseSaccharomyces cerevisiae Proteins

Identifiers

PMID32125828
PMCPMC7310673

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Registered trials

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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.