Evidence map›Paper›PMID 37774000›Full record

ArticleJournal of the American Chemical Society2023

Orthogonal Enzyme-Substrate Design Strategy for Discovery of Human Protein Palmitoyltransferase Substrates.

Robbins Puthenveetil, Shelby A Auger, Natalia Gómez-Navarro, Mitra Shumsher Rana, Riki Das, Liam Brendan Healy, Kiall F Suazo, Zhen-Dan Shi, Rolf E Swenson, Mark D Distefano and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

10 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Mechanisms and functions of protein S-acylation.Nature reviews. Molecular cell biology · 2024
    Review
  8. Bump-hole ZDHHCs.Nature chemical biology · 2024
    Article
  9. Review
  10. 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

11 authors at 2 institutions in 1 country.

Robbins PuthenveetilSection on Structural and Chemical Biology, Neurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20817, United States.
Shelby A AugerDepartment of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455, United States.ORCID 0000-0003-2873-2580
Natalia Gómez-NavarroSection on Structural and Chemical Biology, Neurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20817, United States.
Mitra Shumsher RanaSection on Structural and Chemical Biology, Neurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20817, United States.ORCID 0000-0002-0915-8141
Riki DasDepartment of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455, United States.
Liam Brendan HealySection on Structural and Chemical Biology, Neurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20817, United States.ORCID 0000-0002-2640-1596
Kiall F SuazoDepartment of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455, United States.ORCID 0000-0002-0803-8332
Zhen-Dan ShiThe Chemistry and Synthesis Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Rockville, Maryland 20850, United States.
Rolf E SwensonThe Chemistry and Synthesis Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Rockville, Maryland 20850, United States.
Mark D DistefanoDepartment of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455, United States.ORCID 0000-0002-2872-0259
Anirban BanerjeeSection on Structural and Chemical Biology, Neurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20817, United States.ORCID 0000-0003-1494-6801
National Institutes of Health · USUniversity of Minnesota · US

Funding

Training Grant: Functional Proteomics of AgingT32AG029796 · NIA · UNIVERSITY OF MINNESOTA · PI EDGAR A ARRIAGA, Douglas G Mashek · 2008 to 2026
$6.6M
Training the Next Generation of Chemical BiologistsT32GM132029 · NIGMS · UNIVERSITY OF MINNESOTA · PI Erin Elizabeth Carlson, William Charles Krause Pomerantz · 2019 to 2026
$2.7M
Chemical Approaches for Exploring Protein Prenylation in Living CellsR35GM141853 · NIGMS · UNIVERSITY OF MINNESOTA · PI MARK D DISTEFANO · 2021 to 2026
$2.4M
NIA NIH HHS T32 AG029796NIGMS NIH HHS R35 GM141853NIGMS NIH HHS T32 GM132029
6 · The paper itself

Abstract

Protein palmitoylation, with more than 5000 substrates, is the most prevalent form of protein lipidation. Palmitoylated proteins participate in almost all areas of cellular physiology and have been linked to several human diseases. Twenty-three zDHHC enzymes catalyze protein palmitoylation with extensive overlap among the substrates of each zDHHC member. Currently, there is no global strategy to delineate the physiological substrates of individual zDHHC enzymes without perturbing the natural cellular pool. Here, we outline a general approach to accomplish this on the basis of synthetic orthogonal substrates that are only compatible with engineered zDHHC enzymes. We demonstrate the utility of this strategy by validating known substrates and use it to identify novel substrates of two human zDHHC enzymes. Finally, we employ this method to discover and explore conserved palmitoylation in a family of host restriction factors against pathogenic viruses, including SARS-CoV-2.

Indexed as

AcyltransferasesCOVID-19HumansLipoylationProteinsSARS-CoV-2Substrate SpecificityAcyltransferasesProteins

Identifiers

PMID37774000
PMCPMC10591334
OpenAlexW4387164356

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.