Ya-Qiu Long
National Institutes of Health
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Publication
Featured researches published by Ya-Qiu Long.
Bioorganic & Medicinal Chemistry Letters | 1999
Ya-Qiu Long; Johannes H. Voigt; Feng-Di T. Lung; C.Richter King; Peter P. Roller
Systematic modification of amino acid at position Y-2 of a library-derived non-phosporylated thioether-cyclized peptide, cyclo(CH2CO-Glu2-Leu-Tyr0-Glu-Asn-Val-Gly-Met-Tyr-Cys) -amide, aided by molecular modeling, demonstrates that the Glu(-2) sidechain compensates for the absence of Tyr0 phosphorylation in retaining effective binding to Grb2-SH2 domain. Replacement of Glu(-2) with gamma-carboxyglutamic acid produced a high affinity inhibitor, the first example with submicromolar affinity (IC50 = 640 nM).
Bioorganic & Medicinal Chemistry Letters | 2003
Peng Li; Manchao Zhang; Ya-Qiu Long; Megan L. Peach; Hongpeng Liu; Dajun Yang; Marc C. Nicklaus; Peter P. Roller
Development of Grb2-SH2 domain antagonists is an effective approach to inhibit the growth of malignant cells by modulating Grb2-related Ras signaling. We report here potent Grb2-SH2 domain antagonists that do not rely on phosphotyrosine or its mimics. These non-phosphorylated antagonists were developed and further modified by constraining the backbone conformation and optimizing amino acid side chains of a phage library-derived peptide, G1TE. After extensive SAR studies and structural optimization, non-phosphorylated peptide 12 was discovered with an IC(50) of 75 nM. This potent peptidomimetic provides a novel template for the development of non-pTyr containing Grb2-SH2 domain antagonists and acts as a chemotherapeutic lead for the treatment of erbB2-related cancer.
Archive | 2001
Peter P. Roller; Ya-Qiu Long; Peng Li; Sheau-Ling Lee; Chen-Yong Lin; Istvan J. Enyedy; Shaomeng Wang; Robert B. Dickson
Matriptase is a recently identified type II transmembrane protease that is found on the surface of epithelial cells [1,2]. It is overexpressed in most cancer cells, including human breast cancer cells. It is a multidomain protein with a C-terminal extracellular region containing the protease domain. It activates urokinase-type of plasminogen activator (uPA), and the protease activated receptor (Par-2). It has been demonstrated that matriptase can proteolytically activate hepatocyte growth factor (HGF/Scatter Factor) to its active form, and thus it may function in epithelial cell migration, cancer invasion and metastasis [2]. Developing inhibitors of matriptase provides for a therapeutic approach to metastatic diseases, and in particular, cancer.
Journal of Medicinal Chemistry | 2001
Istvan J. Enyedy; Yan Ling; Kassoum Nacro; York Tomita; Xihan Wu; Yeyu Cao; Ribo Guo; Bihua Li; Xiaofeng Zhu; Ying Huang; Ya-Qiu Long; Peter P. Roller; Dajun Yang; Shaomeng Wang
Journal of Medicinal Chemistry | 2004
Koehler Nk; Chao Yie Yang; Judith Varady; Yipin Lu; Xihan Wu; Meilan Liu; Yin D; Bartels M; Xu By; Peter P. Roller; Ya-Qiu Long; Peng Li; Michael G. Kattah; Cohn Ml; Moran K; Tilley E; Richert; Shaomeng Wang
Journal of Peptide Research | 2001
Feng-Di T. Lung; Ya-Qiu Long; Peter P. Roller; C. R. King; J. Varady; X.‐W. Wu; Shaomeng Wang
Biochemical and Biophysical Research Communications | 1999
Ya-Qiu Long; Zhu-Jun Yao; Johannes H. Voigt; Feng Di T. Lung; Juliet H. Luo; Terrence R. Burke; C. Richter King; Dajun Yang; Peter P. Roller
Archive | 2002
Feng-Di T. Lung; Ya-Qiu Long; Nouri Neamati; Yves Pommier; Peter P. Roller
Archive | 2011
Ya-Qiu Long; Shao-Xu Huang; Zahrah Zawahir; Huiyuan Li; Tino Sanchez; Ying Zhi; Frauke Christ; Zeger Debyser; Nouri Neamati
Archive | 2006
Peter P. Roller; Sheng Jiang; Peng Li; Ya-Qiu Long; Sheau-Ling Lee; Cheng-Yong Lin; Michael Johnson; Richard B. Dickson