Multienzyme Complexes

"Multienzyme Complexes" 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

Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.

Descriptor ID	D009097
MeSH Number(s)	D05.500.562 D08.811.600
Concept/Terms	Multienzyme Complexes Multienzyme Complexes Complexes, Multienzyme

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

Chemicals and Drugs [D]
Macromolecular Substances [D05]
Multiprotein Complexes [D05.500]
Multienzyme Complexes [D05.500.562]
Enzymes and Coenzymes [D08]
Enzymes [D08.811]
Multienzyme Complexes [D08.811.600]

Below are MeSH descriptors whose meaning is related to "Multienzyme Complexes".

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

publications

Timeline | Most Recent

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

Bar chart showing 66 publications over 21 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
1994	3	0	3
1995	3	1	4
1996	4	0	4
1997	2	2	4
1998	1	0	1
1999	2	3	5
2000	1	1	2
2001	1	1	2
2002	5	3	8
2003	4	1	5
2004	3	1	4
2005	4	1	5
2006	1	1	2
2007	2	2	4
2008	2	0	2
2010	1	2	3
2011	1	1	2
2013	2	1	3
2016	1	0	1
2020	0	1	1
2021	0	1	1

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

Verberk SGS, Kuiper KL, Lauterbach MA, Latz E, Van den Bossche J. The multifaceted therapeutic value of targeting ATP-citrate lyase in atherosclerosis. Trends Mol Med. 2021 12; 27(12):1095-1105.

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Goodman RP, Markhard AL, Shah H, Sharma R, Skinner OS, Clish CB, Deik A, Patgiri A, Hsu YH, Masia R, Noh HL, Suk S, Goldberger O, Hirschhorn JN, Yellen G, Kim JK, Mootha VK. Hepatic NADH reductive stress underlies common variation in metabolic traits. Nature. 2020 07; 583(7814):122-126.

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Watanabe S, Peterson CL. Response to Comment on "A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme". Science. 2016 Jul 22; 353(6297):358.

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Kim TY, Jackson S, Xiong Y, Whitsett TG, Lobello JR, Weiss GJ, Tran NL, Bang YJ, Der CJ. CRL4A-FBXW5-mediated degradation of DLC1 Rho GTPase-activating protein tumor suppressor promotes non-small cell lung cancer cell growth. Proc Natl Acad Sci U S A. 2013 Oct 15; 110(42):16868-73.

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Watanabe S, Peterson CL. Chromatin dynamics: flipping the switch on a chromatin remodeling machine. Cell Cycle. 2013 Aug 01; 12(15):2337-8.

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Watanabe S, Radman-Livaja M, Rando OJ, Peterson CL. A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme. Science. 2013 Apr 12; 340(6129):195-9.

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Wernimont SM, Clark AG, Stover PJ, Wells MT, Litonjua AA, Weiss ST, Gaziano JM, Tucker KL, Baccarelli A, Schwartz J, Bollati V, Cassano PA. Folate network genetic variation, plasma homocysteine, and global genomic methylation content: a genetic association study. BMC Med Genet. 2011 Nov 21; 12:150.

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Liu N, Peterson CL, Hayes JJ. SWI/SNF- and RSC-catalyzed nucleosome mobilization requires internal DNA loop translocation within nucleosomes. Mol Cell Biol. 2011 Oct; 31(20):4165-75.

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Berdichevets IN, Tyazhelova TV, Shimshilashvili KhR, Rogaev EI. Lysophosphatidic acid is a lipid mediator with wide range of biological activities. Biosynthetic pathways and mechanism of action. Biochemistry (Mosc). 2010 Sep; 75(9):1088-97.

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O'Brien SK, Cao H, Nathans R, Ali A, Rana TM. P-TEFb kinase complex phosphorylates histone H1 to regulate expression of cellular and HIV-1 genes. J Biol Chem. 2010 Sep 24; 285(39):29713-20.

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