Proteolysis of cystatin C by cathepsin D in the breast cancer microenvironment.
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The Matricellular Receptor LRP1 Forms an Interface for Signaling and Endocytosis in Modulation of the Extracellular Tumor EnvironmentThe lysosome: from waste bag to potential therapeutic targetHuman stefin B role in cell's response to misfolded proteins and autophagyCleavage of Histone 3 by Cathepsin D in the involuting mammary gland.The C-terminal fragment of prostate-specific antigen, a 2331 Da peptide, as a new urinary pathognomonic biomarker candidate for diagnosing prostate cancer.The Importance of Caveolin-1 as Key-Regulator of Three-Dimensional Growth in Thyroid Cancer Cells Cultured under Real and Simulated Microgravity Conditions.Nuclear cathepsin D enhances TRPS1 transcriptional repressor function to regulate cell cycle progression and transformation in human breast cancer cellsProteomic identification of protease cleavage sites: cell-biological and biomedical applications.Cystatin C is a disease-associated protein subject to multiple regulation.Two Faces of Cathepsin D: Physiological Guardian Angel and Pathological Demon.The role of lysosome in cell death regulation.Procathepsin E is highly abundant but minimally active in pancreatic ductal adenocarcinoma tumors.Effects of Rab27a on proliferation, invasion, and anti-apoptosis in human glioma cell.A mechanistic model to predict effects of cathepsin B and cystatin C on β-amyloid aggregation and degradation.Grassystatins D-F, Potent Aspartic Protease Inhibitors from Marine Cyanobacteria as Potential Antimetastatic Agents Targeting Invasive Breast Cancer.Neither creatinine nor cystatin C-estimated glomerular filtration rate is optimal in oncology patients treated with targeted agents.Myocardial Upregulation of Cathepsin D by Ischemic Heart Disease Promotes Autophagic Flux and Protects Against Cardiac Remodeling and Heart Failure.Aberrant cystatin-C expression in blood from patients with breast cancer is a suitable marker for monitoring tumor burdenStructure-Activity Relationships of JMV4463, a Vectorized Cathepsin D Inhibitor with Antiproliferative Properties: The Unique Role of the AMPA-Based Vector
P2860
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P2860
Proteolysis of cystatin C by cathepsin D in the breast cancer microenvironment.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Proteolysis of cystatin C by cathepsin D in the breast cancer microenvironment.
@en
Proteolysis of cystatin C by cathepsin D in the breast cancer microenvironment.
@nl
type
label
Proteolysis of cystatin C by cathepsin D in the breast cancer microenvironment.
@en
Proteolysis of cystatin C by cathepsin D in the breast cancer microenvironment.
@nl
prefLabel
Proteolysis of cystatin C by cathepsin D in the breast cancer microenvironment.
@en
Proteolysis of cystatin C by cathepsin D in the breast cancer microenvironment.
@nl
P2093
P50
P356
P1433
P1476
Proteolysis of cystatin C by cathepsin D in the breast cancer microenvironment
@en
P2093
Christine Prébois
Cédric Oréar
Danielle Derocq
Guillaume Meurice
Magali Gary-Bobo
Magnus Abrahamson
Olivier Masson
Robert E Hollingsworth
Valérie Laurent-Matha
P304
P356
10.1096/FJ.12-205229
P407
P50
P577
2012-08-16T00:00:00Z