Tripartite Motif Proteins

"Tripartite Motif Proteins" 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

A protein family defined by the presence of three ZINC FINGER domains, one of which is a RING FINGER DOMAIN, a coiled-coil region, and a highly variable C-terminal region. They function in many cellular processes including APOPTOSIS and CELL CYCLE regulation.

Descriptor ID	D000070584
MeSH Number(s)	D12.776.934
Concept/Terms	Tripartite Motif Proteins Tripartite Motif Proteins Motif Proteins, Tripartite Proteins, Tripartite Motif RBCC Proteins Proteins, RBCC RBCC Protein Family Family, RBCC Protein Protein Family, RBCC TRIM Protein Family Family, TRIM Protein Protein Family, TRIM TRIM Proteins Proteins, TRIM

Below are MeSH descriptors whose meaning is more general than "Tripartite Motif Proteins".

Chemicals and Drugs [D]
Amino Acids, Peptides, and Proteins [D12]
Proteins [D12.776]
Tripartite Motif Proteins [D12.776.934]

Below are MeSH descriptors whose meaning is related to "Tripartite Motif Proteins".

Below are MeSH descriptors whose meaning is more specific than "Tripartite Motif Proteins".

publications

Timeline | Most Recent

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

Bar chart showing 31 publications over 14 distinct years, with a maximum of 5 publications in 2014

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

Year	Major Topic	Minor Topic	Total
2004	0	1	1
2005	0	1	1
2006	0	4	4
2007	0	1	1
2009	0	3	3
2010	0	3	3
2011	0	3	3
2012	0	4	4
2013	0	1	1
2014	0	5	5
2018	0	1	1
2019	2	0	2
2020	1	0	1
2021	0	1	1

Below are the most recent publications written about "Tripartite Motif Proteins" by people in Profiles.

Naresh NU, Haynes CM. Breaks in mitochondrial DNA rig the immune response. Nature. 2021 03; 591(7850):372-373.

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Ohainle M, Kim K, Komurlu Keceli S, Felton A, Campbell E, Luban J, Emerman M. TRIM34 restricts HIV-1 and SIV capsids in a TRIM5a-dependent manner. PLoS Pathog. 2020 04; 16(4):e1008507.

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Kim K, Dauphin A, Komurlu S, McCauley SM, Yurkovetskiy L, Carbone C, Diehl WE, Strambio-De-Castillia C, Campbell EM, Luban J. Cyclophilin A protects HIV-1 from restriction by human TRIM5a. Nat Microbiol. 2019 12; 4(12):2044-2051.

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Chiramel AI, Meyerson NR, McNally KL, Broeckel RM, Montoya VR, M?ndez-Sol?s O, Robertson SJ, Sturdevant GL, Lubick KJ, Nair V, Youseff BH, Ireland RM, Bosio CM, Kim K, Luban J, Hirsch VM, Taylor RT, Bouamr F, Sawyer SL, Best SM. TRIM5a Restricts Flavivirus Replication by Targeting the Viral Protease for Proteasomal Degradation. Cell Rep. 2019 06 11; 27(11):3269-3283.e6.

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Morger D, Zosel F, B?hlmann M, Z?ger S, Mittelviefhaus M, Schuler B, Luban J, Gr?tter MG. The Three-Fold Axis of the HIV-1 Capsid Lattice Is the Species-Specific Binding Interface for TRIM5a. J Virol. 2018 03 01; 92(5).

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Bhatnagar S, Green MR. TRIMming down tumor suppressors in breast cancer. Cell Cycle. 2015; 14(9):1345-6.

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Bhatnagar S, Gazin C, Chamberlain L, Ou J, Zhu X, Tushir JS, Virbasius CM, Lin L, Zhu LJ, Wajapeyee N, Green MR. TRIM37 is a new histone H2A ubiquitin ligase and breast cancer oncoprotein. Nature. 2014 Dec 04; 516(7529):116-20.

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Uchil PD, Pawliczek T, Reynolds TD, Ding S, Hinz A, Munro JB, Huang F, Floyd RW, Yang H, Hamilton WL, Bewersdorf J, Xiong Y, Calderwood DA, Mothes W. TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly. J Cell Sci. 2014 Sep 15; 127(Pt 18):3928-42.

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Narayan K, Waggoner L, Pham ST, Hendricks GL, Waggoner SN, Conlon J, Wang JP, Fitzgerald KA, Kang J. TRIM13 is a negative regulator of MDA5-mediated type I interferon production. J Virol. 2014 Sep; 88(18):10748-57.

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Yang L, Li R, Kaneko T, Takle K, Morikawa RK, Essex L, Wang X, Zhou J, Emoto K, Xiang Y, Ye B. Trim9 regulates activity-dependent fine-scale topography in Drosophila. Curr Biol. 2014 May 05; 24(9):1024-30.

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