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|a 978-0-387-69056-8
|b Springer
|n http://www.springerlink.com
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|a QP609.P78
|b C36 2008eb
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|b C215 2008
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|2 clc
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049 |
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|a UAMI
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245 |
0 |
4 |
|a The cancer degradome :
|b proteases and cancer biology /
|c Dylan Edwards [and others], editors.
|
246 |
3 |
0 |
|a Proteases and cancer biology
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260 |
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|a New York, NY :
|b Springer,
|c ©2008.
|
300 |
|
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|a 1 online resource (xxiii, 926 pages, 32 unnumbered pages of plates) :
|b illustrations (some color)
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336 |
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|a text
|b txt
|2 rdacontent
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337 |
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|a computer
|b c
|2 rdamedia
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338 |
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|a online resource
|b cr
|2 rdacarrier
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347 |
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|a data file
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504 |
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|a Includes bibliographical references and index.
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520 |
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|a This book will aim to cover recent knowledge of the composition of the Degradome, how it can be studied using modern approaches such as transcriptomics and mass spectrometry; how gene knockout mice have improved our knowledge of the roles of proteases in cancer; how their activity can be imaged both in vitro and in vivo; the links that have emerged between proteolysis and cell signalling; how the degradome can be a useful source of diagnostic and prognostic markers; and finally new approaches to targeting proteolysis for therapy.
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588 |
0 |
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|a Print version record.
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505 |
0 |
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|a The Degradome and Its Analysis -- Protease Genomics and the Cancer Degradome -- The CLIP-CHIP™: A Focused Oligonucleotide Microarray Platform for Transcriptome Analysis of the Complete Human and Murine Cancer Degradomes -- The Hu/Mu ProtIn Chip: A Custom Dual-Species Oligonucleotide Microarray for Profiling Degradome Gene Expression in Tumors and Their Microenvironment -- Quantitative Real-Time PCR Analysis of Degradome Gene Expression -- Identification of Protease Substrates by Mass Spectrometry Approaches-1 -- Identification of Protease Substrates by Mass Spectrometry Approaches-2 -- Activity-Based Imaging and Biochemical Profiling Tools for Analysis of the Cancer Degradome -- Images of Cleavage: Tumor Proteases in Action -- Insights into Protease Function -- Proteolytic Pathways: Intersecting Cascades in Cancer Development -- Physiological Functions of Plasminogen Activation: Effects of Gene Deficiencies in Humans and Mice -- The Plasminogen Activation System in Tissue Remodeling and Cancer Invasion -- The Urokinase Plasminogen Activator Receptor as a Target for Cancer Therapy -- The Endocytic Collagen Receptor, uPARAP/Endo180, in Cancer Invasion and Tissue Remodeling -- Physiological and Pathological Functions of Type II Transmembrane Serine Proteases: Lessons from Transgenic Mouse Models and Human Disease-Associated Mutations -- Roles of Cysteine Proteases in Tumor Progression: Analysis of Cysteine Cathepsin Knockout Mice in Cancer Models -- In Vitro and In Vivo Models of Angiogenesis to Dissect MMP Functions -- The Surface Transplantation Model to Study the Tumor-Host Interface -- Unravelling the Roles of Proteinases in Cell Migration In Vitro and In Vivo -- New Insights into MMP function in Adipogenesis -- TIMPs: Extracellular Modifiers in Cancer Development -- The Interface Between Proteolysis and Cell Signalling -- Invadopodia: Interface for Invasion -- uPAR and Proteases in Mobilization of Hematopoietic Stem Cells -- The Urokinase Receptor and Integrins Constitute a Cell Migration Signalosome -- Measuring uPAR Dynamics in Live Cells -- Janus-Faced Effects of Broad-Spectrum and Specific MMP Inhibition on Metastasis -- Cytokine Substrates: MMP Regulation of Inflammatory Signaling Molecules -- Matrix Metalloproteinases as Key Regulators of Tumor-Bone Interaction -- The Degradome as Source of Cancer Diagnostic and Markers -- The Plasminogen Activation System as a Source of Prognostic Markers in Cancer -- Cysteine Cathepsins and Cystatins as Cancer Biomarkers -- Novel Degradome Markers in Breast Cancer -- Meta-Analysis of Gene Expression Microarray Data: Degradome Genes in Healthy and Cancer Tissues -- Degradome Gene Polymorphisms -- TIMP-1 as a Prognostic Marker in Colorectal Cancer -- Novel Therapeutic Strategies -- Structure and Inhibition of the Urokinase-Type Plasminogen Activator Receptor -- Engineered Antagonists of uPA and PAI-1 -- MMP Inhibitor Clinical Trials -- The Past, Present, and Future -- Tailoring TIMPs for Selective Metalloproteinase Inhibition -- Third-Generation MMP Inhibitors: Recent Advances in the Development of Highly Selective Inhibitors -- Protease-Activated Delivery and Imaging Systems -- Development of Tumour-Selective and Endoprotease-Activated Anticancer Therapeutics -- Targeting Degradome Genes via Engineered Viral Vectors.
|
546 |
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|a English.
|
590 |
|
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|a ProQuest Ebook Central
|b Ebook Central Academic Complete
|
650 |
|
0 |
|a Proteolytic enzymes.
|
650 |
|
0 |
|a Cancer
|x Molecular aspects.
|
650 |
1 |
2 |
|a Peptide Hydrolases
|
650 |
2 |
2 |
|a Neoplasm Invasiveness
|x enzymology
|
650 |
|
6 |
|a Enzymes protéolytiques.
|
650 |
|
6 |
|a Cancer
|x Aspect moléculaire.
|
650 |
|
7 |
|a SCIENCE
|x Life Sciences
|x Biochemistry.
|2 bisacsh
|
650 |
0 |
7 |
|a Cancer
|x Molecular aspects.
|2 cct
|
650 |
0 |
7 |
|a Peptide hydrolases.
|2 cct
|
650 |
0 |
7 |
|a Neoplasm Invasiveness
|x enzymology.
|2 cct
|
650 |
0 |
7 |
|a Proteolytic enzymes.
|2 cct
|
650 |
|
7 |
|a Biomédecine.
|2 eclas
|
650 |
|
7 |
|a Sciences de la vie.
|2 eclas
|
650 |
|
7 |
|a Cancer
|x Molecular aspects
|2 fast
|
650 |
|
7 |
|a Proteolytic enzymes
|2 fast
|
700 |
1 |
|
|a Edwards, Dylan R.
|
758 |
|
|
|i has work:
|a The cancer degradome (Text)
|1 https://id.oclc.org/worldcat/entity/E39PCGDm4fmmX67XvjqxMRJyHP
|4 https://id.oclc.org/worldcat/ontology/hasWork
|
776 |
0 |
8 |
|i Print version:
|t Cancer degradome.
|d New York, NY : Springer, ©2008
|z 9780387690568
|z 0387690565
|w (OCoLC)227032670
|
856 |
4 |
0 |
|u https://ebookcentral.uam.elogim.com/lib/uam-ebooks/detail.action?docID=364191
|z Texto completo
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