Protein Multimerization

"Protein Multimerization" 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

The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS.

Descriptor ID	D055503
MeSH Number(s)	G02.111.694
Concept/Terms	Protein Multimerization Protein Multimerization Multimerization, Protein Protein Multimer Assembly Assembly, Protein Multimer Multimer Assembly, Protein Protein Heteromultimerizaton Protein Heteromultimerizaton Heteromultimerizaton, Protein Heteromultimerizatons, Protein Protein Trimerization Protein Trimerization Trimerization, Protein Protein Dimerization Protein Dimerization Dimerization, Protein

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

Biological Sciences [G]
Chemical Phenomena [G02]
Biochemical Phenomena [G02.111]
Protein Multimerization [G02.111.694]

Below are MeSH descriptors whose meaning is related to "Protein Multimerization".

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

publications

Timeline | Most Recent

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

Bar chart showing 132 publications over 16 distinct years, with a maximum of 16 publications in 2018

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

Year	Major Topic	Minor Topic	Total
2008	0	2	2
2009	3	6	9
2010	2	13	15
2011	2	6	8
2012	2	6	8
2013	2	8	10
2014	2	7	9
2015	3	8	11
2016	0	9	9
2017	1	7	8
2018	1	15	16
2019	0	10	10
2020	1	4	5
2021	0	4	4
2022	0	2	2
2024	0	6	6

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

Dey S, Pahari P, Mukherjee S, Munro JB, Das DK. Conformational dynamics of SARS-CoV-2 Omicron spike trimers during fusion activation at single molecule resolution. Structure. 2024 Nov 07; 32(11):1910-1925.e6.

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Yerramilli VS, Lin G, Reisinger JL, Hemmerlin RM, Lindberg SK, Plante K, Ross AH, Gericke A, Scarlata S. The scaffolding protein IQGAP1 enhances EGFR signaling by promoting oligomerization and preventing degradation. J Biol Chem. 2024 Nov; 300(11):107844.

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Tse-Kang SY, Pukkila-Worley R. Lysosome-related organelle integrity suppresses TIR-1 aggregation to restrain toxic propagation of p38 innate immunity. Cell Rep. 2024 09 24; 43(9):114674.

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Baier AS, Gioacchini N, Eek P, Leith EM, Tan S, Peterson CL. Dual engagement of the nucleosomal acidic patches is essential for deposition of histone H2A.Z by SWR1C. Elife. 2024 May 29; 13.

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Leo G, Leone P, Ataie Kachoie E, Tolomeo M, Galluccio M, Indiveri C, Barile M, Capaldi S. Structural insights into the bifunctional enzyme human FAD synthase. Structure. 2024 Jul 11; 32(7):953-965.e5.

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Yang XY, Shen Z, Xie J, Greenwald J, Marathe I, Lin Q, Xie WJ, Wysocki VH, Fu TM. Molecular basis of Gabija anti-phage supramolecular assemblies. Nat Struct Mol Biol. 2024 Aug; 31(8):1243-1250.

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Erlandsen H, Jecrois AM, Nichols JC, Cole JL, Royer WE. NADH/NAD+ binding and linked tetrameric assembly of the oncogenic transcription factors CtBP1 and CtBP2. FEBS Lett. 2022 02; 596(4):479-490.

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Yang F, Gracia Gervasi M, Orta G, Tourzani DA, De la Vega-Beltr?n JL, Ruthel G, Darszon A, Visconti PE, Wang PJ. C2CD6 regulates targeting and organization of the CatSper calcium channel complex in sperm flagella. Development. 2022 01 15; 149(2).

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Fierle JK, Brioschi M, de Tiani M, Wetterwald L, Atsaves V, Abram-Saliba J, Petrova TV, Coukos G, Dunn SM. Soluble trivalent engagers redirect cytolytic T?cell activity toward tumor endothelial marker 1. Cell Rep Med. 2021 08 17; 2(8):100362.

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Egri SB, Shen K. An interdomain hydrogen bond in the Rag GTPases maintains stable mTORC1 signaling in sensing amino acids. J Biol Chem. 2021 07; 297(1):100861.

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