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Author
- Arcos-Encarnación, Bolivar1
- Cao, Biyin1
- Chakroborty, Deepankar1
- Chiappe, Diego1
- Contreras, Sandra1
- Elenius, Klaus1
- Elo, Laura L1
- Encarnación-Guevara, Sergio1
- Fernandez-Reyes, Francis C1
- Gil, Jeovanis1
- He, Yuanming1
- Jiang, Shuoyi1
- Johnson, Mark S1
- Jänne, Pasi A1
- Koivu, Marika1
- Koivunen, Jussi P1
- Kurppa, Kari J1
- Luna-Peñaloza, Juan1
- Mao, Xinliang1
- Moran, Michael F1
- Ojala, Veera K1
- Paatero, Ilkka1
- Ramírez-Torres, Alberto1
- Tamirat, Mahlet Z1
- Tong, Jiefei1
Keyword
- acetylation1
- anticancer drug1
- cancer biology1
- clonal selection1
- deubiquitylation (deubiquitination)1
- directed evolution1
- driver mutations1
- epidermal growth factor receptor (EGFR)1
- ERBB1
- histone deacetylase inhibitor (HDAC inhibitor) (HDI)1
- multiple myeloma1
- mutagenesis in vitro1
- oncogene1
- passenger mutations1
- sirtuin 1 (SIRT1)1
- somatic evolution1
- stoichiometry1
- targeted therapies1
- transcription factor1
- tyrosine kinase inhibitors1
- tyrosine-protein kinase (tyrosine kinase)1
Genomics and Proteomics
3 Results
- Genomics and ProteomicsOpen Access
The deubiquitinase USP7 stabilizes Maf proteins to promote myeloma cell survival
Journal of Biological ChemistryVol. 295Issue 7p2084–2096Published online: December 10, 2019- Yuanming He
- Siyu Wang
- Jiefei Tong
- Shuoyi Jiang
- Ye Yang
- Zubin Zhang
- and others
Cited in Scopus: 26The Maf proteins, including c-Maf, MafA, and MafB, are critical transcription factors in myelomagenesis. Previous studies demonstrated that Maf proteins are processed by the ubiquitin–proteasome pathway, but the mechanisms remain elusive. This study applied MS to identify MafB ubiquitination-associated proteins and found that the ubiquitin-specific protease USP7 was present in the MafB interactome. Moreover, USP7 also interacted with c-Maf and MafA and blocked their polyubiquitination and degradation. - Editors' PicksOpen Access
An unbiased in vitro screen for activating epidermal growth factor receptor mutations
Journal of Biological ChemistryVol. 294Issue 24p9377–9389Published online: April 5, 2019- Deepankar Chakroborty
- Kari J. Kurppa
- Ilkka Paatero
- Veera K. Ojala
- Marika Koivu
- Mahlet Z. Tamirat
- and others
Cited in Scopus: 8Cancer tissues harbor thousands of mutations, and a given oncogene may be mutated at hundreds of sites, yet only a few of these mutations have been functionally tested. Here, we describe an unbiased platform for the functional characterization of thousands of variants of a single receptor tyrosine kinase (RTK) gene in a single assay. Our in vitro screen for activating mutations (iSCREAM) platform enabled rapid analysis of mutations conferring gain-of-function RTK activity promoting clonal growth. - Genomics and ProteomicsOpen Access
Lysine acetylation stoichiometry and proteomics analyses reveal pathways regulated by sirtuin 1 in human cells
Journal of Biological ChemistryVol. 292Issue 44p18129–18144Published online: September 11, 2017- Jeovanis Gil
- Alberto Ramírez-Torres
- Diego Chiappe
- Juan Luna-Peñaloza
- Francis C. Fernandez-Reyes
- Bolivar Arcos-Encarnación
- and others
Cited in Scopus: 25Lysine acetylation is a widespread posttranslational modification affecting many biological pathways. Recent studies indicate that acetylated lysine residues mainly exhibit low acetylation occupancy, but challenges in sample preparation and analysis make it difficult to confidently assign these numbers, limiting understanding of their biological significance. Here, we tested three common sample preparation methods to determine their suitability for assessing acetylation stoichiometry in three human cell lines, identifying the acetylation occupancy in more than 1,300 proteins from each cell line.