Shi Y, Wan L, Jiao M, Zhong C, Cui H, Yuan J
Nat Commun. 2025; 16(1):2259.
PMID: 40050296
PMC: 11885453.
DOI: 10.1038/s41467-025-57517-y.
Qin Z, Ren H, Zhao P, Wang K, Liu H, Miao C
Brief Bioinform. 2024; 25(6).
PMID: 39316944
PMC: 11421846.
DOI: 10.1093/bib/bbae469.
Murthy D, Attri K, Shukla S, Thakur R, Chaika N, He C
Nat Cell Biol. 2024; 26(4):613-627.
PMID: 38429478
PMC: 11021164.
DOI: 10.1038/s41556-024-01372-4.
Guo X, Liang K, Xia L, Zhang X, Liu J, Wang C
iScience. 2023; 26(12):108446.
PMID: 38034359
PMC: 10687339.
DOI: 10.1016/j.isci.2023.108446.
Rajasheker G, Nagaraju M, Varghese R, Jalaja N, Somanaboina A, Singam P
Front Plant Sci. 2022; 13:952732.
PMID: 36226297
PMC: 9549341.
DOI: 10.3389/fpls.2022.952732.
Targeting the YXXΦ Motifs of the SARS Coronaviruses 1 and 2 ORF3a Peptides by In Silico Analysis to Predict Novel Virus-Host Interactions.
Kakkanas A, Karamichali E, Koufogeorgou E, Kotsakis S, Georgopoulou U, Foka P
Biomolecules. 2022; 12(8).
PMID: 36008946
PMC: 9405953.
DOI: 10.3390/biom12081052.
An acetyltransferase controls the metabolic flux in rubromycin polyketide biosynthesis by direct modulation of redox tailoring enzymes.
Toplak M, Nagel A, Frensch B, Lechtenberg T, Teufel R
Chem Sci. 2022; 13(24):7157-7164.
PMID: 35799824
PMC: 9215129.
DOI: 10.1039/d2sc01952c.
Systematic Characterization of Lysine Post-translational Modification Sites Using MUscADEL.
Chen Z, Liu X, Li F, Li C, Marquez-Lago T, Leier A
Methods Mol Biol. 2022; 2499:205-219.
PMID: 35696083
DOI: 10.1007/978-1-0716-2317-6_11.
Genome-Wide Survey Indicates Diverse Physiological Roles of Calcium-Dependent Protein Kinase Genes.
Yang X, Chen Z, Yin X, Wang Y, Yang Y, Yang Y
Int J Mol Sci. 2022; 23(3).
PMID: 35163223
PMC: 8835911.
DOI: 10.3390/ijms23031298.
De novo variants in H3-3A and H3-3B are associated with neurodevelopmental delay, dysmorphic features, and structural brain abnormalities.
Okur V, Chen Z, Vossaert L, Peacock S, Rosenfeld J, Zhao L
NPJ Genom Med. 2021; 6(1):104.
PMID: 34876591
PMC: 8651650.
DOI: 10.1038/s41525-021-00268-8.
STALLION: a stacking-based ensemble learning framework for prokaryotic lysine acetylation site prediction.
Basith S, Lee G, Manavalan B
Brief Bioinform. 2021; 23(1).
PMID: 34532736
PMC: 8769686.
DOI: 10.1093/bib/bbab376.
MedProDB: A database of Mediator proteins.
Bhardwaj R, Thakur J, Kumar S
Comput Struct Biotechnol J. 2021; 19:4165-4176.
PMID: 34527190
PMC: 8342855.
DOI: 10.1016/j.csbj.2021.07.031.
pathway regulates dietary restriction-dependent enhancement of lifespan in .
Pandey M, Bansal S, Bar S, Yadav A, Sokol N, Tennessen J
Elife. 2021; 10.
PMID: 34100717
PMC: 8233039.
DOI: 10.7554/eLife.62621.
Prediction and analysis of multiple protein lysine modified sites based on conditional wasserstein generative adversarial networks.
Yang Y, Wang H, Li W, Wang X, Wei S, Liu Y
BMC Bioinformatics. 2021; 22(1):171.
PMID: 33789579
PMC: 8010967.
DOI: 10.1186/s12859-021-04101-y.
Chemical Decorations of "MARs" Residents in Orchestrating Eukaryotic Gene Regulation.
Roychowdhury T, Chattopadhyay S
Front Cell Dev Biol. 2021; 8:602994.
PMID: 33409278
PMC: 7779526.
DOI: 10.3389/fcell.2020.602994.
Lysine acetylation of NKG2D ligand Rae-1 stabilizes the protein and sensitizes tumor cells to NKG2D immune surveillance.
Hu J, Xia X, Zhao Q, Li S
Cancer Lett. 2020; 502:143-153.
PMID: 33279621
PMC: 10142196.
DOI: 10.1016/j.canlet.2020.12.002.
Acetylation modulates the Fanconi anemia pathway by protecting FAAP20 from ubiquitin-mediated proteasomal degradation.
Nagareddy B, Khan A, Kim H
J Biol Chem. 2020; 295(40):13887-13901.
PMID: 32763975
PMC: 7535921.
DOI: 10.1074/jbc.RA120.015288.
LMO2 activation by deacetylation is indispensable for hematopoiesis and T-ALL leukemogenesis.
Morishima T, Krahl A, Nasri M, Xu Y, Aghaallaei N, Findik B
Blood. 2019; 134(14):1159-1175.
PMID: 31366618
PMC: 6888148.
DOI: 10.1182/blood.2019000095.
A deep learning method to more accurately recall known lysine acetylation sites.
Wu M, Yang Y, Wang H, Xu Y
BMC Bioinformatics. 2019; 20(1):49.
PMID: 30674277
PMC: 6343287.
DOI: 10.1186/s12859-019-2632-9.
Vertebrate SLRP family evolution and the subfunctionalization of osteoglycin gene duplicates in teleost fish.
Costa R, Martins R, Capilla E, Anjos L, Power D
BMC Evol Biol. 2018; 18(1):191.
PMID: 30545285
PMC: 6293640.
DOI: 10.1186/s12862-018-1310-2.