Evidence map›Paper›PMID 31606079›Full record

ArticleMethods in enzymology2019

Biochemical and structural analysis of N-terminal acetyltransferases.

Leah Gottlieb, Ronen Marmorstein

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 17% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. NADCells · 2025
    Review
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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

2 authors at 1 institution in 1 country.

Leah GottliebDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, United States; Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, United States; Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, United States.
Ronen MarmorsteinDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, United States; Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, United States; Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, United States. Electronic address: marmor@upenn.edu.
University of Pennsylvania · US

Funding

Molecular Mechanisms, Pathways and Inhibition of Acetyl-Transfer ReactionsR35GM118090 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Ronen Marmorstein · 2016 to 2026
$6.7M
Predoctoral Training at the Chemistry-Biology InterfaceT32GM071339 · NIGMS · WISTAR INSTITUTE · PI MARMORSTEIN, RONEN, SPEICHER, DAVID W. · 2005 to 2019
$3.2M
Predoctoral Training at the Chemistry-Biology InterfaceT32GM133398 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Ronen Marmorstein, Ernest James Petersson · 2020 to 2026
$2.4M
NIGMS NIH HHS R35 GM118090NIGMS NIH HHS T32 GM071339NIGMS NIH HHS T32 GM133398
6 · The paper itself

Abstract

N-terminal acetylation is a co- and post-translational modification catalyzed by the conserved N-terminal acetyltransferase (NAT) family of enzymes. A majority of the human proteome is modified by the human NATs (NatA-F and H), which are minimally composed of a catalytic subunit and as many as two auxiliary subunits. Together, NATs specifically regulate many cellular functions by influencing protein activities such as their degradation, membrane targeting, and protein-protein interactions. This chapter will describe methods developed for their preparation, and their biochemical and structural characterization. This will include methodologies for expression and purification of recombinant NAT protein, kinetic assays, biochemical and biophysical assays, and strategies for structural studies.

Indexed as

AnimalsCatalytic DomainCell LineCloning, MolecularCrystallizationCrystallography, X-RayEnzyme AssaysEscherichia coliHumansModels, MolecularN-Terminal AcetyltransferasesProtein ConformationRecombinant ProteinsUp-RegulationN-Terminal AcetyltransferasesRecombinant ProteinsBiophysical analysisCo-translational acetylationNATsN-terminal acetyltransferasesProtein acetyltransferasesProtein complexesX-ray crystallography

Identifiers

PMID31606079
PMCPMC6884420
OpenAlexW2968829898

What OpenQuestion holds

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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.