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Xiang Mao

Researcher at University of Texas MD Anderson Cancer Center

Publications -  6
Citations -  4892

Xiang Mao is an academic researcher from University of Texas MD Anderson Cancer Center. The author has contributed to research in topics: Phosphorylation & Tyrosine phosphorylation. The author has an hindex of 6, co-authored 6 publications receiving 3944 citations. Previous affiliations of Xiang Mao include Nanjing Agricultural University.

Papers
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Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy

Daniel J. Klionsky, +1287 more
- 01 Apr 2012 - 
TL;DR: These guidelines are presented for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
Journal ArticleDOI

Structural bases of unphosphorylated STAT1 association and receptor binding.

Xiang Mao, +9 more
- 18 Mar 2005 - 
TL;DR: Analyses of the wild-type and mutant STAT1 proteins by static light scattering, analytical ultracentrifugation, and coimmunoprecipitation suggest that STAT1 is predominantly dimeric prior to activation, and the dimer is mediated by the ND interactions.
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Implications of an antiparallel dimeric structure of nonphosphorylated STAT1 for the activation–inactivation cycle

Minghao Zhong, +10 more
- 15 Mar 2005 - 
TL;DR: It is concluded that a parallel STAT1 phosphodimer not bound to DNA most likely undergoes a conformational rearrangement to present the phosphotyrosine efficiently for dephosphorylation in vivo and resistance to a tyrosine phosphatase in vitro.
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Crystal structure of unphosphorylated STAT3 core fragment.

Zhiyong Ren, +8 more
- 12 Sep 2008 - 
TL;DR: A 3.05 A-resolution crystal structure of an unphosphorylated STAT3 core fragment is reported, highlighting the structural and biochemical differences between STAT3 and STAT1, and suggesting different regulation mechanisms of these two proteins.
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A Ras Homologue Member I Directly Inhibits Signal Transducers and Activators of Transcription 3 Translocation and Activity in Human Breast and Ovarian Cancer Cells

Arata Nishimoto, +11 more
- 01 Aug 2005 - 
TL;DR: The physical association between STAT3 and ARHI as well as the functional inhibition of STAT3 transcriptional activity by ARHI suggests a novel mechanism through which a putative tumor suppressor gene can inhibit STAT3 activity in breast and ovarian cancers.