Lysine

"Lysine" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure, which enables searching at various levels of specificity.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

An essential amino acid. It is often added to animal feed.

Descriptor ID	D008239
MeSH Number(s)	D12.125.068.555 D12.125.095.647 D12.125.142.497
Concept/Terms	Lysine Lysine L-Lysine L Lysine Lysine Acetate Lysine Acetate Acetate, Lysine Lysine Hydrochloride Lysine Hydrochloride Enisyl Enisyl

Below are MeSH descriptors whose meaning is more general than "Lysine".

Chemicals and Drugs [D]
Amino Acids, Peptides, and Proteins [D12]
Amino Acids [D12.125]
Amino Acids, Basic [D12.125.068]
Lysine [D12.125.068.555]
Amino Acids, Diamino [D12.125.095]
Lysine [D12.125.095.647]
Amino Acids, Essential [D12.125.142]
Lysine [D12.125.142.497]

Below are MeSH descriptors whose meaning is related to "Lysine".

Below are MeSH descriptors whose meaning is more specific than "Lysine".

publications

Timeline | Most Recent

This graph shows the total number of publications written about "Lysine" by people in this website by year, and whether "Lysine" was a major or minor topic of these publications.

Bar chart showing 89 publications over 30 distinct years, with a maximum of 9 publications in 2006

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
1994	1	2	3
1995	0	1	1
1996	0	1	1
1997	0	1	1
1998	0	1	1
1999	1	2	3
2000	0	2	2
2001	1	2	3
2002	0	2	2
2003	2	1	3
2004	3	2	5
2005	1	5	6
2006	4	5	9
2007	1	2	3
2008	1	1	2
2009	1	1	2
2010	3	2	5
2011	1	5	6
2012	1	3	4
2013	2	1	3
2014	0	1	1
2015	1	3	4
2016	1	2	3
2017	2	3	5
2018	0	3	3
2020	0	1	1
2021	0	1	1
2022	0	2	2
2023	2	0	2
2024	1	1	2

Below are the most recent publications written about "Lysine" by people in Profiles.

Fern?ndez-Coto DL, Gil J, Ayala G, Encarnaci?n-Guevara S. Dynamics of Mitochondrial Proteome and Acetylome in Glioblastoma Cells with Contrasting Metabolic Phenotypes. Int J Mol Sci. 2024 Mar 19; 25(6).

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Hu H, Hu W, Guo AD, Zhai L, Ma S, Nie HJ, Zhou BS, Liu T, Jia X, Liu X, Yao X, Tan M, Chen XH. Spatiotemporal and direct capturing global substrates of lysine-modifying enzymes in living cells. Nat Commun. 2024 Feb 17; 15(1):1465.

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Toro TB, Skripnikova EV, Bornes KE, Zhang K, Watt TJ. Endogenous expression of inactive lysine deacetylases reveals deacetylation-dependent cellular mechanisms. PLoS One. 2023; 18(9):e0291779.

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Toro TB, Bornes KE, Watt TJ. Lysine Deacetylase Substrate Selectivity: Distinct Interaction Surfaces Drive Positive and Negative Selection for Residues Following Acetyllysine. Biochemistry. 2023 05 02; 62(9):1464-1483.

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Sapp N, Burge N, Cox K, Prakash P, Balasubramaniam M, Thapa S, Christensen D, Li M, Linderberger J, Kvaratskhelia M, Pandhare J, Craigie R, Poirier MG, Dash C. HIV-1 Preintegration Complex Preferentially Integrates the Viral DNA into Nucleosomes Containing Trimethylated Histone 3-Lysine 36 Modification and Flanking Linker DNA. J Virol. 2022 09 28; 96(18):e0101122.

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G?hmann M, Porter ML, Bok MJ. The Gluopsins: Opsins without the Retinal Binding Lysine. Cells. 2022 08 06; 11(15).

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Toro TB, Swanier JS, Bezue JA, Broussard CG, Watt TJ. Lysine Deacetylase Substrate Selectivity: A Dynamic Ionic Interaction Specific to KDAC8. Biochemistry. 2021 08 24; 60(33):2524-2536.

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Yu R, Wu H, Ismail H, Du S, Cao J, Wang J, Ward T, Yang F, Gui P, Ali M, Chu L, Mo F, Wang Q, Chu Y, Zang J, Zhao Y, Ye M, Fang G, Chen PR, Dou Z, Gao X, Wang W, Liu X, Yao X. Methylation of PLK1 by SET7/9 ensures accurate kinetochore-microtubule dynamics. J Mol Cell Biol. 2020 07 03; 12(6):462-476.

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Almarwani B, Phambu EN, Alexander C, Nguyen HAT, Phambu N, Sunda-Meya A. Vesicles mimicking normal and cancer cell membranes exhibit differential responses to the cell-penetrating peptide Pep-1. Biochim Biophys Acta Biomembr. 2018 Jun; 1860(6):1394-1402.

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McIntosh DJ, Walters TS, Arinze IJ, Davis J. Arkadia (RING Finger Protein 111) Mediates Sumoylation-Dependent Stabilization of Nrf2 Through K48-Linked Ubiquitination. Cell Physiol Biochem. 2018; 46(1):418-430.

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