Evidence map›Paper›PMID 39287128›Full record

ArticleJournal of proteome research2024

Characterizations of Protein Arginine Deiminase 1 as a Substrate of NTMT1: Implications of Nα-Methylation in Protein Stability and Interaction.

Ying Meng, Zhouxian Li, Ming He, Quanqing Zhang, Youchao Deng, Yinsheng Wang, Rong Huang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of proteome research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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.

Ying MengBorch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue Institute for Drug Discovery, Purdue University Center for Cancer Research, Purdue University, 720 Clinic Drive, West Lafayette, Indiana 47907, United States.
Zhouxian LiDepartment of Chemistry, University of California Riverside, 501 Big Springs Road, Riverside, California 92521, United States.
Ming HeBorch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue Institute for Drug Discovery, Purdue University Center for Cancer Research, Purdue University, 720 Clinic Drive, West Lafayette, Indiana 47907, United States.
Quanqing ZhangDepartment of Chemistry, University of California Riverside, 501 Big Springs Road, Riverside, California 92521, United States.
Youchao DengBorch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue Institute for Drug Discovery, Purdue University Center for Cancer Research, Purdue University, 720 Clinic Drive, West Lafayette, Indiana 47907, United States.
Yinsheng WangDepartment of Chemistry, University of California Riverside, 501 Big Springs Road, Riverside, California 92521, United States.
Rong HuangBorch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue Institute for Drug Discovery, Purdue University Center for Cancer Research, Purdue University, 720 Clinic Drive, West Lafayette, Indiana 47907, United States.ORCID 0000-0002-1477-3165

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI Andrea L Kasinski · 1985 to 2026
$43.4M
Chemical Biology of DNA and RNA AlkylationR35ES031707 · NIEHS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI Yinsheng Wang · 2020 to 2026
$6.1M
Protein N-terminal Methylation Mechanisms and InhibitionR01GM117275 · NIGMS · VIRGINIA COMMONWEALTH UNIVERSITY · PI HUANG, RONG · 2016 to 2025
$3.2M
NCI NIH HHS P30 CA023168NIEHS NIH HHS R35 ES031707NIGMS NIH HHS R01 GM117275
6 · The paper itself

Abstract

α-N-Methylation (Nα-methylation), catalyzed by protein N-terminal methyltransferases (NTMTs), constitutes a crucial post-translational modification involving the transfer of a methyl group from

Indexed as

Protein Processing, Post-TranslationalHalf-LifeHEK293 CellsHumansMethylationMethyltransferasesProtein-Arginine DeiminasesProtein-Arginine Deiminase Type 1Protein BindingProtein StabilityProteomicsS-AdenosylmethionineSubstrate SpecificityMethyltransferasesNTMT1 protein, humanProtein-Arginine DeiminasesProtein-Arginine Deiminase Type 1S-AdenosylmethionineNTMT1Nα-methylationPAD1protein−protein interactionsprotein stability

Identifiers

PMID39287128
PMCPMC11452276

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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.