|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Cysteine peptidases, such as cathepsin B and L, take an important role in cancer progression and metastasis.
|
31683457 |
2020 |
|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Cathepsin B plays key roles in tumor progression with its overexpression being associated with invasive and metastatic phenotypes and is a primary target of protease activated antibody-directed prodrug therapy.
|
31493706 |
2019 |
|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Furthermore, the discovery of Cathepsin B secretion and function as an extracellular matrix protein has broadened our appreciation for the impact of Cathepsin B on cancer progression.
|
30796968 |
2019 |
|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Furthermore, we showed that the novel metallodrugs by catB inhibition significantly impair processes of tumor progression in in vitro cell based functional assays at low noncytotoxic concentrations.
|
31464130 |
2019 |
|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
The presented data show that we have further defined the structural requirements for cathepsin B inhibition by nitroxoline derivatives and provided additional knowledge that could lead to non-peptidic compounds with usefulness against tumor progression.
|
29503024 |
2018 |
|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Cathepsin B (CtsB) contributes to atherosclerosis and cancer progression by processing the extracellular matrix and promoting angiogenesis.
|
28904019 |
2018 |
|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Nitroxoline, a known antimicrobial agent, is a potent and selective inhibitor of cathepsin B, hence reducing tumor progression <i>in vitro</i> and <i>in vivo</i>.
|
28938624 |
2017 |
|
Tumor Progression
|
0.100 |
GeneticVariation
|
phenotype |
BEFREE |
This may suggest a possible role of cathepsin B in alterations leading to cancer progression.
|
25808857 |
2016 |
|
Tumor Progression
|
0.100 |
AlteredExpression
|
phenotype |
BEFREE |
Orthotopic transplantation experiments revealed that CTSB overexpression in cancer cells rather than in the stroma affects PyMT tumor progression.
|
24077280 |
2014 |
|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
The results of our study demonstrate the important role of EMMPRIN-2 in head and neck cancer progression for the first time and reveal that increased extracellular secretion of Cathepsin B may be a novel mechanism underlying EMMPRIN-2 enhanced tumor progression in head and neck cancer.
|
24705283 |
2014 |
|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Earlier studies have reported that proteases such as uPA, uPAR and cathepsin B play important roles in tumor progression.
|
21290090 |
2011 |
|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Earlier studies have reported important roles of uPA, uPAR and cathepsin B in tumor progression.
|
21347260 |
2011 |
|
Tumor Progression
|
0.100 |
AlteredExpression
|
phenotype |
BEFREE |
Overall, our results indicate that CSC activates cathepsin B and L proteolytic activity and enhances invasiveness in OSCC cells, a response that may play a role in CSC-mediated tumor progression and metastasis dissemination.
|
17399918 |
2007 |
|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Earlier studies have reported that the cysteine protease cathepsin B and the matrix metalloproteinase MMP-9 play important roles in tumor progression.
|
17912429 |
2007 |
|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Based upon these results, we speculate that cathepsin B, a protease implicated in tumor progression, plays a functional role in initiating proteolytic cascades in caveolae as downstream components of this cascade (e.g., urokinase plasminogen activator and urokinase plasminogen activator receptor) are also present in HCT 116 caveolae.
|
14965444 |
2004 |
|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
The cysteine proteinase cathepsin B has been implicated in tumor progression by virtue of its increased mRNA and protein levels, as well as its localization at the invading front of the tumor.
|
14730346 |
2004 |
|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Here we focus on the molecular regulation of cathepsin B and attendant implications for tumor progression and arthritis.
|
12887051 |
2003 |
|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
The lysosomal cysteine protease cathepsin B has been implicated in tumor progression and metastasis in part due to its altered trafficking.
|
10849765 |
2000 |
|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Cysteine protease cathepsin B (CatB) and its endogenous inhibitor stefin A (StA) play an important role in tumor progression.
|
10653164 |
2000 |
|
Tumor Progression
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Cathepsin B (CB) is involved in degradation of extracellular matrix proteins during tumor progression in human solid organ tumors (such as colorectal, bladder, and breast cancers), including human prostate cancer.
|
10652560 |
2000 |
|
Tumor Progression
|
0.100 |
AlteredExpression
|
phenotype |
BEFREE |
These results indicate that the expression of CB in gastric carcinoma is related to tumor progression, and leads to development of the invasive phenotype.
|
11155666 |
1998 |
|
Tumor Progression
|
0.100 |
AlteredExpression
|
phenotype |
BEFREE |
The majority of reports on cathepsin B expression in tumors have focused on measurements of activity or protein staining.In some tumors, e.g. gliomas, a correlation between the amounts of cathepsin B mRNA, protein and activity and tumor progression has been established.
|
8861022 |
1996 |