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Chenghua Yang
Researcher at Second Military Medical University
Publications - 18
Citations - 885
Chenghua Yang is an academic researcher from Second Military Medical University. The author has contributed to research in topics: Cancer & Prostate cancer. The author has an hindex of 10, co-authored 15 publications receiving 668 citations. Previous affiliations of Chenghua Yang include Cornell University & Kettering University.
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Journal ArticleDOI
MALT1 Small Molecule Inhibitors Specifically Suppress ABC-DLBCL In Vitro and In Vivo
Lorena Fontan,Lorena Fontan,Chenghua Yang,Venkataraman Kabaleeswaran,Venkataraman Kabaleeswaran,Venkataraman Kabaleeswaran,Laurent Volpon,Michael J. Osborne,Elena Beltran,Monica Garcia,Leandro Cerchietti,Rita Shaknovich,Shao Ning Yang,Fang Fang,Randy D. Gascoyne,Jose A. Martinez-Climent,J. Fraser Glickman,Katherine L. B. Borden,Hao Wu,Hao Wu,Hao Wu,Ari Melnick +21 more
TL;DR: A selected lead compound, MI-2, featured direct binding to MALT1 and suppression of its protease function and was nontoxic to mice, and displayed selective activity against ABC-DLBCL cell lines in vitro and xenotransplanted ABC- DLBCL tumors in vivo.
Journal ArticleDOI
The epichaperome is an integrated chaperome network that facilitates tumour survival
Anna Rodina,Tai Wang,Pengrong Yan,Erica DaGama Gomes,Mark Dunphy,Nagavarakishore Pillarsetty,John Koren,John F. Gerecitano,Tony Taldone,Hongliang Zong,Eloisi Caldas-Lopes,Mary L. Alpaugh,Adriana D. Corben,Matthew Riolo,Brad Beattie,Christina Pressl,Radu I Peter,Chao Xu,Robert Trondl,Hardik J. Patel,Fumiko Shimizu,Alexander Bolaender,Chenghua Yang,Palak Panchal,Mohammad F. Farooq,Sarah Kishinevsky,Shanu Modi,Oscar Lin,Feixia Chu,Sujata Patil,Hediye Erdjument-Bromage,Pat Zanzonico,Clifford A. Hudis,Lorenz Studer,Gail J. Roboz,Ethel Cesarman,Leandro Cerchietti,Ross L. Levine,Ari Melnick,Steven M. Larson,Jason S. Lewis,Monica L. Guzman,Gabriela Chiosis,Gabriela Chiosis +43 more
TL;DR: It is found that under conditions of stress, such as malignant transformation fuelled by MYC, the chaperome becomes biochemically ‘rewired’ to form a network of stable, survival-facilitating, high-molecular-weight complexes.
Journal ArticleDOI
Structural architecture of the CARMA1/Bcl10/MALT1 signalosome: nucleation-induced filamentous assembly.
Qi Qiao,Chenghua Yang,Chao Zheng,Lorena Fontan,Liron David,Liron David,Xiong Yu,Clay Bracken,Monica Rosen,Ari Melnick,Edward H. Egelman,Hao Wu,Hao Wu,Hao Wu +13 more
TL;DR: It is shown that the reconstituted CBM signalosome is a helical filamentous assembly in which substoichiometric CARMA1 nucleates Bcl10 filaments, supporting a paradigm of nucleation-induced signal transduction with threshold response due to cooperativity and signal amplification by polymerization.
Journal ArticleDOI
A genomic and epigenomic atlas of prostate cancer in Asian populations.
Jing Li,Chuanliang Xu,Hyung Joo Lee,Shancheng Ren,Xiaoyuan Zi,Zhiming Zhang,Haifeng Wang,Yongwei Yu,Chenghua Yang,Chenghua Yang,Xiaofeng Gao,Jianguo Hou,Linhui Wang,Bo Yang,Qing Yang,Huamao Ye,Tie Zhou,Xin Lu,Yan Wang,Min Qu,Qingsong Yang,Wenhui Zhang,Nakul M. Shah,Erica C. Pehrsson,Shuo Wang,Zengjun Wang,Jun Jiang,Yan Zhu,Rui Chen,Huan Chen,Feng Zhu,Bijun Lian,Xiaoyun Li,Yun Zhang,Chao Wang,Yue Wang,Guangan Xiao,Junfeng Jiang,Yue Yang,Chaozhao Liang,Jian-quan Hou,Conghui Han,Ming Chen,Ning Jiang,Dahong Zhang,Song Wu,Jinjian Yang,Tao Wang,Yongliang Chen,Jiantong Cai,Wenzeng Yang,Jun Xu,Shaogang Wang,Xu Gao,Ting Wang,Yinghao Sun +55 more
TL;DR: Genomic, transcriptomic and DNA methylation data from tissue samples from 208 Chinese patients with prostate cancer define the landscape of alterations in this population, and comparison with data from Western cohorts suggests that the disease may stratify into different molecular subtypes.
Journal ArticleDOI
Biophysical analysis and small-angle X-ray scattering-derived structures of MeCP2–nucleosome complexes
TL;DR: It is demonstrated that MeCP2 forms defined complexes with nucleosomes, in which all four histones are present, and SAXS studies revealed unexpected sequence-dependent conformational variability in the nucleosome themselves.