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 45 publications over 14 distinct years, with a maximum of 9 publications in 2015

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

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

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

McNamar R, Rothblum K, Rothblum LI. The Mammalian and Yeast A49 and A34 Heterodimers: Homologous but Not the Same. Genes (Basel). 2021 04 22; 12(5).

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Berndt N, Bippes CC, Michalk I, Bachmann D, Bachmann J, Puentes-Cala E, Bartsch T, Loureiro LR, Kegler A, Bergmann R, Gross JK, Gross T, Kurien BT, Scofield RH, Farris AD, James JA, Schmitz M, Fahmy K, Feldmann A, Arndt C, Bachmann MP. Two Be or Not Two Be: The Nuclear Autoantigen La/SS-B Is Able to Form Dimers and Oligomers in a Redox Dependent Manner. Int J Mol Sci. 2021 Mar 25; 22(7).

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Knutson BA, McNamar R, Rothblum LI. Dynamics of the RNA polymerase I TFIIF/TFIIE-like subcomplex: a mini-review. Biochem Soc Trans. 2020 10 30; 48(5):1917-1927.

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Chakraborty D, Strayve DG, Makia MS, Conley SM, Kakahel M, Al-Ubaidi MR, Naash MI. Novel molecular mechanisms for Prph2-associated pattern dystrophy. FASEB J. 2020 01; 34(1):1211-1230.

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Zulliger R, Conley SM, Mwoyosvi ML, Al-Ubaidi MR, Naash MI. Oligomerization of Prph2 and Rom1 is essential for photoreceptor outer segment formation. Hum Mol Genet. 2018 10 15; 27(20):3507-3518.

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Skinner OS, Haverland NA, Fornelli L, Melani RD, Do Vale LHF, Seckler HS, Doubleday PF, Schachner LF, Srzentic K, Kelleher NL, Compton PD. Top-down characterization of endogenous protein complexes with native proteomics. Nat Chem Biol. 2018 Jan; 14(1):36-41.

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Kim SK, Barron L, Hinck CS, Petrunak EM, Cano KE, Thangirala A, Iskra B, Brothers M, Vonberg M, Leal B, Richter B, Kodali R, Taylor AB, Du S, Barnes CO, Sulea T, Calero G, Hart PJ, Hart MJ, Demeler B, Hinck AP. An engineered transforming growth factor ß (TGF-ß) monomer that functions as a dominant negative to block TGF-ß signaling. J Biol Chem. 2017 04 28; 292(17):7173-7188.

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Conley SM, Stuck MW, Watson JN, Naash MI. Rom1 converts Y141C-Prph2-associated pattern dystrophy to retinitis pigmentosa. Hum Mol Genet. 2017 02 01; 26(3):509-518.

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Lawrence SL, Gorman MA, Feil SC, Mulhern TD, Kuiper MJ, Ratner AJ, Tweten RK, Morton CJ, Parker MW. Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent Cytolysins. Structure. 2016 09 06; 24(9):1488-98.

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Stuck MW, Conley SM, Naash MI. RDS Functional Domains and Dysfunction in Disease. Adv Exp Med Biol. 2016; 854:217-22.

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