Cullin Proteins

"Cullin 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 family of structurally related proteins that were originally discovered for their role in cell-cycle regulation in CAENORHABDITIS ELEGANS. They play important roles in regulation of the CELL CYCLE and as components of UBIQUITIN-PROTEIN LIGASES.

Descriptor ID	D044842
MeSH Number(s)	D08.811.464.938.750.750.500 D12.776.167.175
Concept/Terms	Cullin Proteins Cullin Proteins Cullin Domain Proteins Cullins Cullin Domain Protein Cullin Protein

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

Chemicals and Drugs [D]
Enzymes and Coenzymes [D08]
Enzymes [D08.811]
Ligases [D08.811.464]
Ubiquitin-Protein Ligase Complexes [D08.811.464.938]
Ubiquitin-Protein Ligases [D08.811.464.938.750]
SKP Cullin F-Box Protein Ligases [D08.811.464.938.750.750]
Cullin Proteins [D08.811.464.938.750.750.500]
Amino Acids, Peptides, and Proteins [D12]
Proteins [D12.776]
Cell Cycle Proteins [D12.776.167]
Cullin Proteins [D12.776.167.175]

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

publications

Timeline | Most Recent

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

Bar chart showing 11 publications over 10 distinct years, with a maximum of 2 publications in 2005

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

Year	Major Topic	Minor Topic	Total
2003	1	0	1
2005	2	0	2
2008	0	1	1
2010	1	0	1
2013	0	1	1
2014	1	0	1
2015	1	0	1
2016	1	0	1
2022	1	0	1
2023	1	0	1

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

Zhao S, Olmayev-Yaakobov D, Ru W, Li S, Chen X, Zhang J, Yao X, Koren I, Zhang K, Xu C. Molecular basis for C-degron recognition by CRL2APPBP2 ubiquitin ligase. Proc Natl Acad Sci U S A. 2023 Oct 24; 120(43):e2308870120.

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Kawamura A, Yoshida S, Aoki K, Shimoyama Y, Yamada K, Yoshida K. DYRK2 maintains genome stability via neddylation of cullins in response to DNA damage. J Cell Sci. 2022 06 01; 135(11).

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Fu W, Sun J, Huang G, Liu JC, Kaufman A, Ryan RJ, Ramanathan SY, Venkatesh T, Singh B. Squamous Cell Carcinoma-related Oncogene (SCCRO) Family Members Regulate Cell Growth and Proliferation through Their Cooperative and Antagonistic Effects on Cullin Neddylation. J Biol Chem. 2016 Mar 18; 291(12):6200-17.

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Carbone M, Gaudino G, Yang H. Recent insights emerging from malignant mesothelioma genome sequencing. J Thorac Oncol. 2015 Mar; 10(3):409-11.

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Guo G, Chmielecki J, Goparaju C, Heguy A, Dolgalev I, Carbone M, Seepo S, Meyerson M, Pass HI. Whole-exome sequencing reveals frequent genetic alterations in BAP1, NF2, CDKN2A, and CUL1 in malignant pleural mesothelioma. Cancer Res. 2015 Jan 15; 75(2):264-9.

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Pozzebon ME, Varadaraj A, Mattoscio D, Jaffray EG, Miccolo C, Galimberti V, Tommasino M, Hay RT, Chiocca S. BC-box protein domain-related mechanism for VHL protein degradation. Proc Natl Acad Sci U S A. 2013 Nov 05; 110(45):18168-73.

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Gao D, Wan L, Inuzuka H, Berg AH, Tseng A, Zhai B, Shaik S, Bennett E, Tron AE, Gasser JA, Lau A, Gygi SP, Harper JW, DeCaprio JA, Toker A, Wei W. Rictor forms a complex with Cullin-1 to promote SGK1 ubiquitination and destruction. Mol Cell. 2010 Sep 10; 39(5):797-808.

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Miranda-Carboni GA, Krum SA, Yee K, Nava M, Deng QE, Pervin S, Collado-Hidalgo A, Galic Z, Zack JA, Nakayama K, Nakayama KI, Lane TF. A functional link between Wnt signaling and SKP2-independent p27 turnover in mammary tumors. Genes Dev. 2008 Nov 15; 22(22):3121-34.

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Luo K, Xiao Z, Ehrlich E, Yu Y, Liu B, Zheng S, Yu XF. Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G. Proc Natl Acad Sci U S A. 2005 Aug 09; 102(32):11444-9.

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Liu B, Sarkis PT, Luo K, Yu Y, Yu XF. Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase. J Virol. 2005 Aug; 79(15):9579-87.

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