Cancer invasion and tissue remodeling--cooperation of protease systems and cell types.
about
Matriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivoMalignant myoepithelial cells are associated with the differentiated papillary structure and metastatic ability of a syngeneic murine mammary adenocarcinoma modelMetalloproteinases: role in breast carcinogenesis, invasion and metastasisC766T low-density lipoprotein receptor-related protein 1 (LRP1) gene polymorphism and susceptibility to breast cancerThe nuclear factor kappa B inhibitor parthenolide restores ICI 182,780 (Faslodex; fulvestrant)-induced apoptosis in antiestrogen-resistant breast cancer cells.Plasminogen Activator System and Breast Cancer: Potential Role in Therapy Decision Making and Precision MedicineHER2 and uPAR cooperativity contribute to metastatic phenotype of HER2-positive breast cancerTargets of fibroblast growth factor 1 (FGF-1) and FGF-2 signaling involved in the invasive and tumorigenic behavior of carcinoma cellsNeutralisation of uPA with a monoclonal antibody reduces plasmin formation and delays skin wound healing in tPA-deficient miceSelective abrogation of the uPA-uPAR interaction in vivo reveals a novel role in suppression of fibrin-associated inflammationPhenotypic overlap between MMP-13 and the plasminogen activation system during wound healing in mice.Deregulated matriptase causes ras-independent multistage carcinogenesis and promotes ras-mediated malignant transformation.Targeted disruption of mouse fibroblast activation protein.Human retinal pigment epithelial lysis of extracellular matrix: functional urokinase plasminogen activator receptor, collagenase, and elastaseMatriptase is involved in ErbB-2-induced prostate cancer cell invasionPotent antitumor activity of a urokinase-activated engineered anthrax toxin.Urokinase-type plasminogen activator and its receptor synergize to promote pathogenic proteolysis.Targeting NF-κB in infantile hemangioma-derived stem cells reduces VEGF-A expression.MMP9 is protective against lethal inflammatory mass lesions in the mouse colon.Host plasminogen activator inhibitor-1 promotes human skin carcinoma progression in a stage-dependent manner.Plasminogen activation independent of uPA and tPA maintains wound healing in gene-deficient mice.Protease nexin-1 expression is altered in human breast cancer.Deficiency for the cysteine protease cathepsin L promotes tumor progression in mouse epidermisCellular activation of the self-quenched fluorescent reporter probe in tumor microenvironment.Plasminogen activator promotes recovery following spinal cord injuryCirculating soluble urokinase plasminogen activator receptor is stably elevated during the first week of treatment in the intensive care unit and predicts mortality in critically ill patientsMembrane associated proteases and their inhibitors in tumour angiogenesis.An anthrax toxin variant with an improved activity in tumor targetingProteolytic-antiproteolytic balance and its regulation in carcinogenesis.Dissecting the urokinase activation pathway using urokinase-activated anthrax toxin.PEGylated DX-1000: pharmacokinetics and antineoplastic activity of a specific plasmin inhibitor.Phospho-MEK1/2 and uPAR Expression Determine Sensitivity of AML Blasts to a Urokinase-Activated Anthrax Lethal Toxin (PrAgU2/LF).Intracellular collagen degradation mediated by uPARAP/Endo180 is a major pathway of extracellular matrix turnover during malignancy.The topology of plasminogen binding and activation on the surface of human breast cancer cellsIntermolecular complementation achieves high-specificity tumor targeting by anthrax toxinPreparation and antitumor effect of a toxin-linked conjugate targeting vascular endothelial growth factor receptor and urokinase plasminogen activator.Solid tumor therapy by selectively targeting stromal endothelial cells.Signaling through urokinase and urokinase receptor in lung cancer cells requires interactions with beta1 integrins.Role of plasminogen activator in spinal cord remodeling after spinal cord injury.Transforming growth factor-Beta and urokinase-type plasminogen activator: dangerous partners in tumorigenesis-implications in skin cancer.
P2860
Q24672921-0AE139ED-9A4C-4640-8B3F-213D96A55BD1Q24794341-164FDCC6-8D97-44E6-A057-733A95F6DCEDQ24803225-86DF9ABF-0543-4C6E-879D-9EB5BD06149EQ24803584-19A0C91C-3B8A-4A89-A039-16F9791C2770Q24815528-F5D4BB50-6CD9-4DB3-A358-2DA5392585C2Q28067626-D535DF70-8B8C-4AB4-ABD7-4A20FD6A6386Q28085413-20D613B7-181C-4DA0-A9F1-9D712347FBA1Q28575842-662B8D46-5611-45F6-B360-672C06BC3A56Q28749280-1096D046-1490-434F-8524-DA41ABBD249EQ30496585-07FF1EF4-B638-4E0D-8C9E-1C0AA373CFFDQ33822269-6A8ED0C5-BC54-428B-BC71-02AE81918462Q33917709-5E2DE4E1-2D70-4001-922C-43D90B708248Q33961797-5B118793-3F34-4D04-A32F-DDB7125DEBE0Q34330943-37A8EF92-3200-44DA-A2B1-687B39ABCEF6Q34358331-232E81F9-041F-4361-80EB-596D7B96EA59Q34470439-4F1F0C5C-F1F5-4431-AA98-9BE4BE1F4C93Q34489359-5592BC0B-5A4B-452E-BFB2-248EBD18A180Q34555267-680B769E-C008-44E9-9A1C-DC0A9E7F8140Q34611765-BA1A4C86-5A98-47FB-8C0E-D3243B7C8254Q34725029-6D596A35-5BE9-4A7C-9221-88DC1EF7327CQ34766934-CE068DA1-03AC-4375-8050-5F59B435B30AQ34768102-76B22F82-D3C4-436F-8B50-5E53836517A6Q34859485-84B85F07-8ADD-461A-87EC-7C897C0B298EQ34929009-660357CF-655F-4CAB-A9BD-673CB70470FDQ35136587-758F4F56-8F11-4D4B-B5B1-D0004A9DFB5FQ35567020-20C432C9-CAD4-469F-ADD6-02437156F2BCQ35587684-1ED02D64-DBC7-4909-BAED-E038ACA9191EQ35846297-AAA7476B-5A32-44CE-9DAF-56A05BE03C4DQ36068428-E10BD8B8-7595-42F9-AB85-4378D5D3203EQ36086826-000899B8-F78F-48D9-B790-BC0B08B611CAQ36143607-FCA271F9-822B-4FC0-9FDD-9C901C9A2EBFQ36243031-85813D63-9DA1-4189-8804-2B7067096BC9Q36321204-DA9338B3-33F0-49BA-A2F7-9DE7CDCB2CD3Q36643348-78F16351-8029-4A54-912D-861851D2D466Q36688750-80F9C484-69F0-4AAB-93B0-B044710A992CQ37071261-F3531510-C715-4D28-8A5E-A413AE363025Q37102436-17D62149-8169-4D7D-B5B5-22C098C7003FQ37520525-70071310-2EB7-494D-8555-B466F772817FQ37570790-1CAED68F-4283-4EDB-93A7-BFC8CEFD211FQ38132176-8808D62C-4BD9-4DFE-9C0C-161E2EFD6F8F
P2860
Cancer invasion and tissue remodeling--cooperation of protease systems and cell types.
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Cancer invasion and tissue remodeling--cooperation of protease systems and cell types.
@ast
Cancer invasion and tissue remodeling--cooperation of protease systems and cell types.
@en
Cancer invasion and tissue remodeling--cooperation of protease systems and cell types.
@nl
type
label
Cancer invasion and tissue remodeling--cooperation of protease systems and cell types.
@ast
Cancer invasion and tissue remodeling--cooperation of protease systems and cell types.
@en
Cancer invasion and tissue remodeling--cooperation of protease systems and cell types.
@nl
prefLabel
Cancer invasion and tissue remodeling--cooperation of protease systems and cell types.
@ast
Cancer invasion and tissue remodeling--cooperation of protease systems and cell types.
@en
Cancer invasion and tissue remodeling--cooperation of protease systems and cell types.
@nl
P2093
P1476
Cancer invasion and tissue remodeling--cooperation of protease systems and cell types
@en
P2093
B S Nielsen
P304
P356
10.1111/J.1699-0463.1999.TB01534.X
P577
1999-01-01T00:00:00Z