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Angus Chen, Ph.D. - Publications

Affiliations: 
2002 Icahn School of Medicine at Mount Sinai, New York, NY, United States 
Area:
Biochemistry, Cell Biology, Molecular Biology
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10 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2003 Wu K, Yamoah K, Dolios G, Gan-Erdene T, Tan P, Chen A, Lee CG, Wei N, Wilkinson KD, Wang R, Pan ZQ. DEN1 is a dual function protease capable of processing the C terminus of Nedd8 and deconjugating hyper-neddylated CUL1. The Journal of Biological Chemistry. 278: 28882-91. PMID 12759363 DOI: 10.1074/Jbc.M302888200  0.614
2002 Macip S, Igarashi M, Fang L, Chen A, Pan ZQ, Lee SW, Aaronson SA. Inhibition of p21-mediated ROS accumulation can rescue p21-induced senescence. The Embo Journal. 21: 2180-8. PMID 11980715 DOI: 10.1093/Emboj/21.9.2180  0.478
2002 Chen A, Kleiman FE, Manley JL, Ouchi T, Pan ZQ. Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase. The Journal of Biological Chemistry. 277: 22085-92. PMID 11927591 DOI: 10.1074/Jbc.M201252200  0.582
2002 Wu K, Chen A, Tan P, Pan ZQ. The Nedd8-conjugated ROC1-CUL1 core ubiquitin ligase utilizes Nedd8 charged surface residues for efficient polyubiquitin chain assembly catalyzed by Cdc34. The Journal of Biological Chemistry. 277: 516-27. PMID 11675391 DOI: 10.1074/Jbc.M108008200  0.567
2001 Kentsis A, Dwyer EC, Perez JM, Sharma M, Chen A, Pan ZQ, Borden KLB. The RING domains of the promyelocytic leukemia protein PML and the arenaviral protein Z repress translation by directly inhibiting translation initiation factor eIF4E Journal of Molecular Biology. 312: 609-623. PMID 11575918 DOI: 10.1006/Jmbi.2001.5003  0.551
2000 Wu K, Chen A, Pan ZQ. Conjugation of Nedd8 to CUL1 enhances the ability of the ROC1-CUL1 complex to promote ubiquitin polymerization. The Journal of Biological Chemistry. 275: 32317-24. PMID 10921923 DOI: 10.1074/Jbc.M004847200  0.602
2000 Chen A, Wu K, Fuchs SY, Tan P, Gomez C, Pan ZQ. The conserved RING-H2 finger of ROC1 is required for ubiquitin ligation. The Journal of Biological Chemistry. 275: 15432-9. PMID 10748083 DOI: 10.1074/Jbc.M907300199  0.587
2000 Wu K, Fuchs SY, Chen A, Tan P, Gomez C, Ronai Z, Pan ZQ. The SCF(HOS/beta-TRCP)-ROC1 E3 ubiquitin ligase utilizes two distinct domains within CUL1 for substrate targeting and ubiquitin ligation. Molecular and Cellular Biology. 20: 1382-93. PMID 10648623 DOI: 10.1128/Mcb.20.4.1382-1393.2000  0.609
1999 Fuchs SY, Chen A, Xiong Y, Pan ZQ, Ronai Z. HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IkappaB and beta-catenin. Oncogene. 18: 2039-46. PMID 10321728 DOI: 10.1038/Sj.Onc.1202760  0.562
1999 Tan P, Fuchs SY, Chen A, Wu K, Gomez C, Ronai Z, Pan ZQ. Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha. Molecular Cell. 3: 527-33. PMID 10230406 DOI: 10.1016/S1097-2765(00)80481-5  0.536
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