Evidence map›Paper›PMID 32111884›Full record

ArticleScientific reports2020

Examining sterically demanding lysine analogs for histone lysine methyltransferase catalysis.

Abbas H K Al Temimi, Vu Tran, Ruben S Teeuwen, Arthur J Altunc, Helene I V Amatdjais-Groenen, Paul B White, Danny C Lenstra, Giordano Proietti, Yali Wang, Anita Wegert and 5 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

5 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Substrate Scope for Human Histone Lysine Acetyltransferase KAT8.International journal of molecular sciences · 2021
    Article
  3. Trimethyllysine: From Carnitine Biosynthesis to Epigenetics.International journal of molecular sciences · 2020
    Review
  4. Article
  5. 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

15 authors at 5 institutions in 4 countries.

Abbas H K Al TemimiInstitute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ, Nijmegen, The Netherlands.
Vu TranInstitute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ, Nijmegen, The Netherlands.
Ruben S TeeuwenInstitute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ, Nijmegen, The Netherlands.
Arthur J AltuncInstitute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ, Nijmegen, The Netherlands.
Helene I V Amatdjais-GroenenInstitute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ, Nijmegen, The Netherlands.
Paul B WhiteInstitute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ, Nijmegen, The Netherlands.
Danny C LenstraInstitute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ, Nijmegen, The Netherlands.
Giordano ProiettiDepartment of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230, Odense, Denmark.
Yali WangInstitute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ, Nijmegen, The Netherlands.
Anita WegertMercachem B.V., Kerkenbos 1013, 6546 BB, Nijmegen, The Netherlands.
Richard H BlaauwChiralix B.V., Kerkenbos 1013, 6546 BB, Nijmegen, The Netherlands.
Ping QianChemistry and Material Science Faculty, Shandong Agricultural University, 271018, Tai'an, Shandong, P.R. China.
Wansheng RenChemistry and Material Science Faculty, Shandong Agricultural University, 271018, Tai'an, Shandong, P.R. China.
Hong GuoDepartment of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, TN, 37996, USA. hguo1@utk.edu.
Jasmin MecinovićInstitute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ, Nijmegen, The Netherlands. mecinovic@sdu.dk.
Radboud University Nijmegen · NLShandong Agricultural University · CNUniversity of Southern Denmark · DKJilin University · CNUniversity of Tennessee at Knoxville · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methylation of lysine residues in histone proteins is catalyzed by S-adenosylmethionine (SAM)-dependent histone lysine methyltransferases (KMTs), a genuinely important class of epigenetic enzymes of biomedical interest. Here we report synthetic, mass spectrometric, NMR spectroscopic and quantum mechanical/molecular mechanical (QM/MM) molecular dynamics studies on KMT-catalyzed methylation of histone peptides that contain lysine and its sterically demanding analogs. Our synergistic experimental and computational work demonstrates that human KMTs have a capacity to catalyze methylation of slightly bulkier lysine analogs, but lack the activity for analogs that possess larger aromatic side chains. Overall, this study provides an important chemical insight into molecular requirements that contribute to efficient KMT catalysis and expands the substrate scope of KMT-catalyzed methylation reactions.

Indexed as

CatalysisCatalytic DomainHistone-Lysine N-MethyltransferaseHumansLysineHistone-Lysine N-MethyltransferaseLysine

Identifiers

PMID32111884
PMCPMC7048932
OpenAlexW3009333840

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.