Výsledky vyhledávání - "Hyun I, Park"

Effects of detergents on catalytic activity of human endometase/matrilysin 2, a putative cancer biomarker

Autor: Seakwoo Lee, Qing-Xiang Amy Sang, Qiang Cao, Asad Ullah, Hyun I. Park

Publikováno v: Analytical biochemistry. 396(2)

Matrix metalloproteinases (MMPs) are a family of hydrolytic enzymes that play significant roles in development, morphogenesis, inflammation, and cancer invasion. Endometase (matrilysin 2 or MMP-26) is a putative early biomarker for human carcinomas.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a93beb089c1b7fd3e561d0dfdee14bef
https://pubmed.ncbi.nlm.nih.gov/19818727

Zobrazit plný text záznamu

Calcium regulates tertiary structure and enzymatic activity of human endometase/matrilysin-2 and its role in promoting human breast cancer cell invasion

Autor: Qing-Xiang Amy Sang, Hyun I. Park, Seakwoo Lee

Publikováno v: The Biochemical journal. 403(1)

Human MMP-26 (matrix metalloproteinase-26) (also known as endometase or matrilysin-2) is a putative biomarker for human carcinomas of breast, prostate and other cancers of epithelial origin. Calcium modulates protein structure and function and may ac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7dc7be281f733f40d0e5936fa12ee12e
https://pubmed.ncbi.nlm.nih.gov/17176253

Zobrazit plný text záznamu

Endometase/matrilysin-2 in human breast ductal carcinoma in situ and its inhibition by tissue inhibitors of metalloproteinases-2 and -4: a putative role in the initiation of breast cancer invasion

Autor: Yun-Ge, Zhao, Ai-Zhen, Xiao, Hyun I, Park, Robert G, Newcomer, Mei, Yan, Yan-Gao, Man, Sue C, Heffelfinger, Qing-Xiang Amy, Sang

Publikováno v: Cancer research. 64(2)

Local disruption of the integrity of both the myoepithelial cell layer and the basement membrane is an indispensable prerequisite for the initiation of invasion and the conversion of human breast ductal carcinoma in situ (DCIS) to infiltrating ductal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cafc9c33e63c1ef00477f178b0b5083f
https://pubmed.ncbi.nlm.nih.gov/14744773

Zobrazit plný text záznamu

The intermediate S1' pocket of the endometase/matrilysin-2 active site revealed by enzyme inhibition kinetic studies, protein sequence analyses, and homology modeling

Autor: Yonghao Jin, Martin A. Schwartz, Seakwoo Lee, Douglas R. Hurst, Hyun I. Park, Qing-Xiang Amy Sang, Cyrus A. Monroe

Publikováno v: The Journal of biological chemistry. 278(51)

Human matrix metalloproteinase-26 (MMP-26/endometase/matrilysin-2) is a newly identified MMP and its structure has not been reported. The enzyme active site S1′ pocket in MMPs is a well defined substrate P1′ amino acid residue-binding site with v

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b97f09726da8f981e3fd073602fbc3e
https://pubmed.ncbi.nlm.nih.gov/14532275

Zobrazit plný text záznamu

Autolytic processing at Glu586-Ser587 within the cysteine-rich domain of human adamalysin 19/disintegrin-metalloproteinase 19 is necessary for its proteolytic activity

Autor: Hyun I. Park, Yun Ge Zhao, Harald Tschesche, Qing-Xiang Amy Sang, Yewseok Suh, Tie-Bang Kang

Publikováno v: The Journal of biological chemistry. 277(50)

We investigated the regulation of the proteolytic activity of human adamalysin 19 (a disintegrin and metalloproteinase 19, hADAM19). It was processed at Glu(586) (P1)-Ser(587)(P1') site in the cysteine-rich domain as shown by protein N-terminal seque

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4241c3e400a7a398b721573dac0947a2
https://pubmed.ncbi.nlm.nih.gov/12393862

Zobrazit plný text záznamu

Peptide substrate specificities and protein cleavage sites of human endometase/matrilysin-2/matrix metalloproteinase-26

Autor: Lewis C. Cantley, Qing-Xiang Amy Sang, Ferry E. Gerkema, Hyun I. Park, Benjamin E. Turk

Publikováno v: The Journal of biological chemistry. 277(38)

Human endometase/matrilysin-2/matrix metalloproteinase-26 (MMP-26) is a novel epithelial and cancer-specific metalloproteinase. Peptide libraries were used to profile the substrate specificity of MMP-26 from the P4-P4' sites. The optimal cleavage mot

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be7f52312256c045571dbaee4f2cdd9d
https://pubmed.ncbi.nlm.nih.gov/12119297

Zobrazit plný text záznamu

Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor

Autor: Ding Liu, Qing-Xiang Amy Sang, Ferry E. Gerkema, Vladimir E. Belozerov, Jian Ni, Hyun I. Park

Publikováno v: The Journal of biological chemistry. 275(27)

We report the discovery, cloning, and characterization of a novel human matrix metalloproteinase 26 (MMP-26) (matrixin) gene, endometase, an endometrial tumor-derived metalloproteinase. Among more than three million expressed sequence tags sequenced,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::082793d88191a9fc5d012f3059c5391c
https://pubmed.ncbi.nlm.nih.gov/10801841

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání