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Search Results to Thomas Kelly Jr

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One or more keywords matched the following items that are connected to Kelly Jr, Thomas

Item TypeName
Academic Article Seprase, a membrane-bound protease, is overexpressed by invasive ductal carcinoma cells of human breast cancers.
Academic Article Fibroblast activation protein-alpha and dipeptidyl peptidase IV (CD26): cell-surface proteases that activate cell signaling and are potential targets for cancer therapy.
Concept Membrane Proteins
Academic Article Fibroblast activation protein-a: a key modulator of the microenvironment in multiple pathologies.
Academic Article Fibroblast activation protein-a promotes tumor growth and invasion of breast cancer cells through non-enzymatic functions.
Academic Article DPPIV, seprase, and related serine peptidases in multiple cellular functions.
Academic Article A potential marker protease of invasiveness, seprase, is localized on invadopodia of human malignant melanoma cells.
Academic Article Membrane proteases as potential diagnostic and therapeutic targets for breast malignancy.
Academic Article Evaluation of seprase activity.
Academic Article Seprase, a membrane-bound protease, alleviates the serum growth requirement of human breast cancer cells.
Academic Article Seprase complexes in cellular invasiveness.
Academic Article Nonerythrocyte spectrins: actin-membrane attachment proteins occurring in many cell types.
Academic Article Proteins involved in the attachment of actin to the plasma membrane.
Academic Article Binding and localization of M(r) 72,000 matrix metalloproteinase at cell surface invadopodia.
Academic Article Cleavage of Type I Collagen by Fibroblast Activation Protein-a Enhances Class A Scavenger Receptor Mediated Macrophage Adhesion.
Academic Article VT68.2: An Antibody to Chondroitin Sulfate Proteoglycan 4 (CSPG4) Displays Reactivity against a Tumor-Associated Carbohydrate Antigen.
Academic Article HDL-associated estradiol stimulates endothelial NO synthase and vasodilation in an SR-BI-dependent manner.

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  • Membrane Proteins