Ligases

"Ligases" 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

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A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.

Descriptor ID	D008025
MeSH Number(s)	D08.811.464
Concept/Terms	Ligases Ligases Synthetases Synthetase

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

Chemicals and Drugs [D]
Enzymes and Coenzymes [D08]
Enzymes [D08.811]
Ligases [D08.811.464]

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

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

publications

Timeline | Most Recent

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

Bar chart showing 21 publications over 11 distinct years, with a maximum of 8 publications in 2002

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

Year	Major Topic	Minor Topic	Total
1995	0	1	1
1998	2	1	3
2000	1	0	1
2001	1	0	1
2002	6	2	8
2003	0	1	1
2016	1	0	1
2018	1	0	1
2019	1	0	1
2020	1	0	1
2023	0	2	2

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

Padhy AA, Mavor D, Sahoo S, Bolon DNA, Mishra P. Systematic profiling of dominant ubiquitin variants reveals key functional nodes contributing to evolutionary selection. Cell Rep. 2023 09 26; 42(9):113064.

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Kreutzfeld O, Tumwebaze PK, Okitwi M, Orena S, Byaruhanga O, Katairo T, Conrad MD, Rasmussen SA, Legac J, Aydemir O, Giesbrecht D, Forte B, Campbell P, Smith A, Kano H, Nsobya SL, Blasco B, Duffey M, Bailey JA, Cooper RA, Rosenthal PJ. Susceptibility of Ugandan Plasmodium falciparum Isolates to the Antimalarial Drug Pipeline. Microbiol Spectr. 2023 06 15; 11(3):e0523622.

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Sch?fer H, Beckert B, Frese CK, Steinchen W, Nuss AM, Beckstette M, Hantke I, Driller K, Sudzinov? P, Kr?sn? L, Kaever V, Dersch P, Bange G, Wilson DN, Turgay K. The alarmones (p)ppGpp are part of the heat shock response of Bacillus subtilis. PLoS Genet. 2020 03; 16(3):e1008275.

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Lariviere PJ, Mahone CR, Santiago-Collazo G, Howell M, Daitch AK, Zeinert R, Chien P, Brown PJB, Goley ED. An Essential Regulator of Bacterial Division Links FtsZ to Cell Wall Synthase Activation. Curr Biol. 2019 05 06; 29(9):1460-1470.e4.

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Chen Q, Huang L, Pan D, Zhu LJ, Wang YX. Cbx4 Sumoylates Prdm16 to Regulate Adipose Tissue Thermogenesis. Cell Rep. 2018 03 13; 22(11):2860-2872.

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Loveland AB, Bah E, Madireddy R, Zhang Y, Brilot AF, Grigorieff N, Korostelev AA. Ribosome?RelA structures reveal the mechanism of stringent response activation. Elife. 2016 07 19; 5.

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Bach I, Ostendorff HP. Orchestrating nuclear functions: ubiquitin sets the rhythm. Trends Biochem Sci. 2003 Apr; 28(4):189-95.

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Otis CN, Krebs PA, Albuquerque A, Quezado MM, San Juan X, Sobel ME, Merino MJ. Loss of heterozygosity of p53, BRCA1, VHL, and estrogen receptor genes in breast carcinoma: correlation with related protein products and morphologic features. Int J Surg Pathol. 2002 Oct; 10(4):237-45.

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Zhou MI, Wang H, Ross JJ, Kuzmin I, Xu C, Cohen HT. The von Hippel-Lindau tumor suppressor stabilizes novel plant homeodomain protein Jade-1. J Biol Chem. 2002 Oct 18; 277(42):39887-98.

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Haynes CM, Caldwell S, Cooper AA. An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport. J Cell Biol. 2002 Jul 08; 158(1):91-101.

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