๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

In situ hybridization studies of metalloproteinases 2 and 9 and TIMP-1 and TIMP-2 expression in human prostate cancer

โœ Scribed by M. Wood; K. Fudge; J. L. Mohler; A. R. Frost; F. Garcia; Min Wang; M. E. Stearns


Book ID
110370151
Publisher
Springer
Year
1997
Tongue
English
Weight
497 KB
Volume
15
Category
Article
ISSN
0262-0898

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Differential regulation of matrix metall
โœ Zhong Dong; Jeffrey A. Nemeth; Michael L. Cher; Kenneth C. Palmer; Robert C. Bri ๐Ÿ“‚ Article ๐Ÿ“… 2001 ๐Ÿ› John Wiley and Sons ๐ŸŒ French โš– 298 KB

Tumor-stromal interactions have been suggested to be a critical factor in both tumor invasion and tumor metastasis. Here, we examined the role of tumor-stromal interactions using co-cultures of prostate cancer (PC) cells derived from primary and metastatic tumors with primary or immortalized stromal

Adenovirus-mediated expression of TIMP-1
โœ Xiyun Deng; Guangchun He; Andrea Levine; Ya Cao; Chad Mullins ๐Ÿ“‚ Article ๐Ÿ“… 2007 ๐Ÿ› John Wiley and Sons ๐ŸŒ French โš– 699 KB

## Abstract Matrix metalloproteinases (MMPs) are proteolytic enzymes that play critical roles in the pathogenesis of human cancers. Clinical trials using synthetic small molecule MMP inhibitors have been carried out but with little success. Tissue inhibitors of metalloproteinases (TIMPs) are endoge

Enhanced RNA expression of tissue inhibi
โœ Hitoshi Yoshiji; Daniel E. Gomez; Unnur P. Thorgeirsson ๐Ÿ“‚ Article ๐Ÿ“… 1996 ๐Ÿ› John Wiley and Sons ๐ŸŒ French โš– 408 KB ๐Ÿ‘ 2 views

Tissue inhibitor of metalloproteinases-I (TIMP-I) is known to have at least 2 distinct types of activity, i.e., as a regulator of collagenolytic activity, and erythroid potentiating activity (EPA). In this study, we examined the expression of TIMP-I in human mammary carcinomas, non-malignant breast