Extracellular Matrix: Pathobiology and Signaling / / ed. by Nikos Karamanos.
Over the last decades cell biology and biological chemistry have increasingly turned their attention to the space between cells and revealed an elaborate network of macromolecules essential for structural support, cell adhesion and signaling. This comprehensive handbook of the extracellular matrix w...
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Superior document: | Title is part of eBook package: De Gruyter DGBA Backlist Complete English Language 2000-2014 PART1 |
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Place / Publishing House: | Berlin ;, Boston : : De Gruyter, , [2012] ©2012 |
Year of Publication: | 2012 |
Language: | English |
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Physical Description: | 1 online resource (888 p.) |
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Extracellular Matrix: Pathobiology and Signaling / ed. by Nikos Karamanos. Berlin ; Boston : De Gruyter, [2012] ©2012 1 online resource (888 p.) text txt rdacontent computer c rdamedia online resource cr rdacarrier text file PDF rda Frontmatter -- Contents -- Preface -- Comments on the book Extracellular Matrix: Pathobiology & Signaling -- About the Editor/Section Editors -- List of contributing authors -- Abbreviations and acronyms used -- 1 An introduction to the extracellular matrix molecules and their importance in pathobiology and signaling -- 1.1 Extracellular matrix: a functional scaffold -- 2 Insights into the function of glycans -- 2.1 Introduction -- 2.2 Metabolic control of hyaluronan synthesis -- 2.3 Multiple roles of hyaluronan as a target and modifier of the inflammatory response -- 2.4 Roles of sulfated and nonsulfated glycosaminoglycans in cancer growth and progression-therapeutic implications -- 2.5 Heparan sulfate design: regulation of biosynthesis -- 2.6 Bone and skin disorders caused by a disturbance in the biosynthesis of chondroitin sulfate and dermatan sulfate -- 2.7 Biological functions of branched N-glycans related to physiology and pathology of extracellular matrix -- 3 Proteoglycans: structure, pathobiology, and signaling -- 3.1 Introduction -- 3.2 Aggrecan in skeletal development and regenerative medicine -- 3.3 The pathobiology of versican -- 3.4 The biology of perlecan and its bioactive modules -- 3.5 Small leucine-rich proteoglycans: multifunctional signaling effectors -- 3.6 Structure and function of syndecans -- 3.7 The glypican family -- 3.8 Serglycin proteoglycan: implications for thrombosis, inflammation, atherosclerosis, and metastasis -- 4 Matrix Proteinases: biological significance in health and disease -- 4.1 Introduction -- 4.2 Extracellular functions of cysteine proteases -- 4.3 Plasmin and the plasminogen activator system in health and disease -- 4.4 Matrix metalloproteinase complexes and their biological significance -- 4.5 The ADAMTS family of metalloproteinases -- 4.6 Proteinases in wound healing -- 4.7 Rock, paper, and molecular scissors: regulating the game of extracellular matrix homeostasis, remodeling, and inflammation -- 5 ECM cell surface receptors -- 5.1 Introduction -- 5.2 Integrin function in heart fibrosis: mechanical strain, transforming growth factor-beta 1 activation, and collagen glycation -- 5.3 Cancer-associated fibroblast integrins as therapeutic targets in the tumor microenvironment -- 5.4 Discoidin domain receptors: non-integrin collagen receptors on the move -- 5.5 Syndecans as receptors for pericellular molecules -- 5.6 CD44: a Sensor of tissue damage critical for restoring homeostasis -- 6 Collagens: insights into the folding, assembly and functions -- 6.1 Introduction -- 6.2 Trimerization domains in collagens: chain selection, folding initiation, and triple-helix stabilization -- 6.3 Structural basis of collagen missense mutations -- 6.4 Roles and regulation of BMP1/Tolloid-like proteinases: collagen/matrix assembly, growth factor activation, and beyond -- 6.5 Supramolecular assembly of type I collagen -- 6.6 Collagen interactomes: mapping functional domains and mutations on fibrillar and network-forming collagens -- 6.7 Collagen-binding proteins -- 7 Emerging aspects in extracellular matrix pathobiology -- 7.1 Introduction -- 7.2 Extracellular matrix in breast cancer: permissive and restrictive influences emanating from the stroma -- 7.3 EMMPRIN/CD147: potential functions in tumor microenvironment and therapeutic target for human cancer -- 7.4 Implication of hyaluronidases in cancer growth, metastasis, diagnosis, and treatment -- 7.5 Structure-function relationship of syndecan-1, with focus on nuclear translocation and tumor cell behavior -- 7.6 Serglycin: a novel player in the terrain of neoplasia -- 7.7 Quantifying cell-ECM pathobiology in 3D -- 7.8 Diabetic foot infections -- 8 Targeting tumor microenvironment at the ECM level -- 8.1 Introduction -- 8.2 Targeting the tumor microenvironment in cancer progression -- 8.3 Growth factor signaling and extracellular matrix -- 8.4 Targeting protein-glycan interactions at cell surface during EMT and hematogenous metastasis: consequences on tumor invasion and metastasis -- 8.5 Pharmacological targeting of proteoglycans and metalloproteinases: an emerging aspect in cancer treatment -- 8.6 Targeting syndecan shedding in cancer -- 8.7 PG receptors with phosphatase action in cancer and angiogenesis -- 8.8 Heparanase, a multifaceted protein involved in cancer, chronic inflammation, and kidney dysfunction -- 8.9 Delivery systems targeting cancer at the level of ECM -- Index restricted access http://purl.org/coar/access_right/c_16ec online access with authorization star Over the last decades cell biology and biological chemistry have increasingly turned their attention to the space between cells and revealed an elaborate network of macromolecules essential for structural support, cell adhesion and signaling. This comprehensive handbook of the extracellular matrix will give an overview of the current state of knowledge of matrix components (structure and function), their role in heath and disease (matrix pathobiology) and new aspects related to pharmacological targeting.It will provide an introduction to the extracellular matrix and detailed sections and chapters on: Importance of extracellular matrix in health and disease Matrix proteoglycans (aggrecan, versican, perlecan, SLRPs, syndecans, glypicans, serglycin) Matrix proteinases (remodeling, would healing, regulatory roles in health and disease, metalloproteinases, cystein proteases, plasmin and plasminogen activator system) Glycobiology (hyaluronan and sulfated glycosaminoglycans in cancer, inflammation and metabolic control) Collagens (supramolecular assembly, proteins binding collagen, scaffolds, bacterial and mutated collagens, procollagen proteinases) Cell surface receptors (integrins, syndecans, mechanical strain and TGFb, CD44 and DDR). Biotechnological and pharmacological outlook (matrix regulation by growth factors, hyaluronidases, pathobiology, disease targeting, delivery systems, EMT and proteomics). "The book Extracellular Matrix: Pathobiology and Signaling provides a comprehensive and up to date collection of very relevant topics for understanding the various facets of extracellular matrix and its interactions with cells in normal tissue as well as in disease. It represents the current front-line and will serve as a reference for extracellular matrix and posttranslational modifications." Dick Heinegård, Department of Clinical Sciences Lund, Section Rheumatology, Lund University, Sweden Over the last decades cell biology and biological chemistry have increasingly turned their attention to the space between cells and revealed an elaborate network of macromolecules essential for structural support, cell migration, adhesion and signaling. This comprehensive handbook of the extracellular matrix is organized into seven thematic sections, giving an overview of the current state of knowledge of matrix components (structure and function), their roles in health and disease (matrix pathobiology) as well as new concepts of pharmacological targeting. Mode of access: Internet via World Wide Web. In English. Description based on online resource; title from PDF title page (publisher's Web site, viewed 30. Aug 2021) Cellular signal transduction. Extracellular matrix Pathophysiology. Extracellular matrix Physiology. Biochemie. Glykane. Kollagene. Matrix. Metalloproteinasen. SCIENCE / Life Sciences / Biochemistry. bisacsh Biochemistry. Collagens. Glycans. Metalloproteinases. Afratis, Nikos, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Aletras, Alexios J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Bell, Rebecca, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Bendeck, Michelle P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Berdiaki, Aikaterini, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Boudko, Sergei P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Bouga, Helen, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Brakebusch, Cord, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Brodsky, Barbara, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Bächinger, Hans Peter, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Capurro, Mariana, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Casu, Benito, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Couchman, John R., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Dagälv, Anders, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb De Luca, Giancarlo, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Deligny, Audrey, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Des Parkin, J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Do, Anh-Tri, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Dobra, Katalin, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Dufour, Antoine, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Elkin, Michael, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Fadnes, Bodil, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Filmus, Jorge, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Filou, Serafoula, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Gabison, Eric E, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Gao, Congxiao, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ghatak, Shibnath, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Gialeli, Chrisostomi, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Gorski, Daniel J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Gu, Jianguo, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Gullberg, Donald, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Gullberg, Donald. Hadler-Olsen, Elin, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hascall, Vincent C., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hascall, Vincent, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Heinegård, Dick, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Heldin, Paraskevi, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hinz, Boris, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hjerpe, Anders, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Huet, Eric, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hulmes, David J. S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ilan, Neta, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Iozzo, Renato V., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Jacenko, Olena, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Jokela, Tiina A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Karamanos, Nikos K., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Karamanos, Nikos, editor. edt http://id.loc.gov/vocabulary/relators/edt Karousou, Evgenia, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kjelle, Lena, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kletsas, Dimitris, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kolliopoulos, Constantine, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Korpetinou, Angeliki, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Koutsioumpa, Marina, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kovalszky, Ilona, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kozlowski, Eliene O., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kähäri, Veli-Matti, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Labropoulou, Vassiliki, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Li, Jin-Ping, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lu, Ning, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Maffei, Joseph S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Magnussen, Synnøve, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Markwald, Roger R., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb McCulloch, Christopher A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb McNicols, Colton, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Menashi, Suzanne, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Merline, Rosetta, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Milia-Argeiti, Eleni, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Misra, Suniti, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Mizumoto, Shuji, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Moali, Catherine, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Mourah, Samia, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nagase, Hideaki, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nastase, Madalina V., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nikitovic, Dragana, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ohtsubo, Kazuaki, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Oikari, Sanna, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Orgel, Joseph P. R. O., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Overall, Christopher M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Papadimitriou, Evangelia, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Paraskevi, Heldin. Passi, Alberto, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Pataki, Csilla, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Pavao, Mauro S. G., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Persikov, Anton V., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Pikas, Dagmar S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Plaas, Anna, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Pratsinis, Harris, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Pucci-Minafra, Ida, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Puré, Ellen, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Raspanti, Mario, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Rocca, Antonio S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Rydén, Cecilia, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb San Antonio, James D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Sanderson, Ralph D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Sandy, John, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Sasaki, Takako, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Savige, Judy, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Schaefer, Liliana, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Schaefer, Liliana. Schick, Barbara P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Skandalis, Spyros S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Solberg, Rigmor, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Sugahara, Kazuyuki, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Svineng, Gunbjørg, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Sylte, Ingebrigt, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Tammi, Markku I., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Tammi, Raija H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Taniguchi, Naoyuki, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Teixeira, Felipe C.O.B., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Tenni, Ruggero, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Tenni, Ruggero. Theocharis, Achilleas D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Theocharis, Achilleas, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Theocharis, Achilleas. Thidemann Johansen, Harald, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Toriseva, Mervi, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Triantaphyllidou, Irene-Eva, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Tsegenidis, Theodore, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Tzanakakis, George N., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Uhlin-Hansen, Lars, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Velasco, Jennifer, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Vigetti, Davide, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Viola, Manuela, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Vlodavsky, Israel, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Vynios, Demitrios H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Wang, Vincent, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Whiteford, James R., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Wight, Thomas N., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Willis, Chris D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Winberg, Jan-Olof, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Winberg, Jan-Olof. Xian, Xiaojie, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Zaman, Muhammad H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Zong, Fang, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Title is part of eBook package: De Gruyter DGBA Backlist Complete English Language 2000-2014 PART1 9783110238570 Title is part of eBook package: De Gruyter DGBA Backlist Medicine and Life Sciences 2000-2014 (EN) 9783110238495 Title is part of eBook package: De Gruyter DGBA Medicine and Life Sciences 2000 - 2014 9783110637915 ZDB-23-GML Title is part of eBook package: De Gruyter E-BOOK GESAMTPAKET / COMPLETE PACKAGE 2012 9783110288995 ZDB-23-DGG Title is part of eBook package: De Gruyter E-BOOK PACKAGE BIOLOGY, CHEMISTRY, GEOSCIENCES 2012 9783110294071 ZDB-23-DBE Title is part of eBook package: De Gruyter E-BOOK PAKET BIOLOGIE, CHEMIE, GEOWISS. 2012 9783110294064 ZDB-23-DBC print 9783110258769 https://doi.org/10.1515/9783110258776 https://www.degruyter.com/isbn/9783110258776 Cover https://www.degruyter.com/cover/covers/9783110258776.jpg |
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Afratis, Nikos, Afratis, Nikos, Aletras, Alexios J., Aletras, Alexios J., Bell, Rebecca, Bell, Rebecca, Bendeck, Michelle P., Bendeck, Michelle P., Berdiaki, Aikaterini, Berdiaki, Aikaterini, Boudko, Sergei P., Boudko, Sergei P., Bouga, Helen, Bouga, Helen, Brakebusch, Cord, Brakebusch, Cord, Brodsky, Barbara, Brodsky, Barbara, Bächinger, Hans Peter, Bächinger, Hans Peter, Capurro, Mariana, Capurro, Mariana, Casu, Benito, Casu, Benito, Couchman, John R., Couchman, John R., Dagälv, Anders, Dagälv, Anders, De Luca, Giancarlo, De Luca, Giancarlo, Deligny, Audrey, Deligny, Audrey, Des Parkin, J., Des Parkin, J., Do, Anh-Tri, Do, Anh-Tri, Dobra, Katalin, Dobra, Katalin, Dufour, Antoine, Dufour, Antoine, Elkin, Michael, Elkin, Michael, Fadnes, Bodil, Fadnes, Bodil, Filmus, Jorge, Filmus, Jorge, Filou, Serafoula, Filou, Serafoula, Gabison, Eric E, Gabison, Eric E, Gao, Congxiao, Gao, Congxiao, Ghatak, Shibnath, Ghatak, Shibnath, Gialeli, Chrisostomi, Gialeli, Chrisostomi, Gorski, Daniel J., Gorski, Daniel J., Gu, Jianguo, Gu, Jianguo, Gullberg, Donald, Gullberg, Donald, Gullberg, Donald. Hadler-Olsen, Elin, Hadler-Olsen, Elin, Hascall, Vincent C., Hascall, Vincent C., Hascall, Vincent, Hascall, Vincent, Heinegård, Dick, Heinegård, Dick, Heldin, Paraskevi, Heldin, Paraskevi, Hinz, Boris, Hinz, Boris, Hjerpe, Anders, Hjerpe, Anders, Huet, Eric, Huet, Eric, Hulmes, David J. S., Hulmes, David J. S., Ilan, Neta, Ilan, Neta, Iozzo, Renato V., Iozzo, Renato V., Jacenko, Olena, Jacenko, Olena, Jokela, Tiina A., Jokela, Tiina A., Karamanos, Nikos K., Karamanos, Nikos K., Karamanos, Nikos, Karamanos, Nikos, Karousou, Evgenia, Karousou, Evgenia, Kjelle, Lena, Kjelle, Lena, Kletsas, Dimitris, Kletsas, Dimitris, Kolliopoulos, Constantine, Kolliopoulos, Constantine, Korpetinou, Angeliki, Korpetinou, Angeliki, Koutsioumpa, Marina, Koutsioumpa, Marina, Kovalszky, Ilona, Kovalszky, Ilona, Kozlowski, Eliene O., Kozlowski, Eliene O., Kähäri, Veli-Matti, Kähäri, Veli-Matti, Labropoulou, Vassiliki, Labropoulou, Vassiliki, Li, Jin-Ping, Li, Jin-Ping, Lu, Ning, Lu, Ning, Maffei, Joseph S., Maffei, Joseph S., Magnussen, Synnøve, Magnussen, Synnøve, Markwald, Roger R., Markwald, Roger R., McCulloch, Christopher A., McCulloch, Christopher A., McNicols, Colton, McNicols, Colton, Menashi, Suzanne, Menashi, Suzanne, Merline, Rosetta, Merline, Rosetta, Milia-Argeiti, Eleni, Milia-Argeiti, Eleni, Misra, Suniti, Misra, Suniti, Mizumoto, Shuji, Mizumoto, Shuji, Moali, Catherine, Moali, Catherine, Mourah, Samia, Mourah, Samia, Nagase, Hideaki, Nagase, Hideaki, Nastase, Madalina V., Nastase, Madalina V., Nikitovic, Dragana, Nikitovic, Dragana, Ohtsubo, Kazuaki, Ohtsubo, Kazuaki, Oikari, Sanna, Oikari, Sanna, Orgel, Joseph P. R. O., Orgel, Joseph P. R. O., Overall, Christopher M., Overall, Christopher M., Papadimitriou, Evangelia, Papadimitriou, Evangelia, Paraskevi, Heldin. Passi, Alberto, Passi, Alberto, Pataki, Csilla, Pataki, Csilla, Pavao, Mauro S. G., Pavao, Mauro S. G., Persikov, Anton V., Persikov, Anton V., Pikas, Dagmar S., Pikas, Dagmar S., Plaas, Anna, Plaas, Anna, Pratsinis, Harris, Pratsinis, Harris, Pucci-Minafra, Ida, Pucci-Minafra, Ida, Puré, Ellen, Puré, Ellen, Raspanti, Mario, Raspanti, Mario, Rocca, Antonio S., Rocca, Antonio S., Rydén, Cecilia, Rydén, Cecilia, San Antonio, James D., San Antonio, James D., Sanderson, Ralph D., Sanderson, Ralph D., Sandy, John, Sandy, John, Sasaki, Takako, Sasaki, Takako, Savige, Judy, Savige, Judy, Schaefer, Liliana, Schaefer, Liliana, Schaefer, Liliana. Schick, Barbara P., Schick, Barbara P., Skandalis, Spyros S., Skandalis, Spyros S., Solberg, Rigmor, Solberg, Rigmor, Sugahara, Kazuyuki, Sugahara, Kazuyuki, Svineng, Gunbjørg, Svineng, Gunbjørg, Sylte, Ingebrigt, Sylte, Ingebrigt, Tammi, Markku I., Tammi, Markku I., Tammi, Raija H., Tammi, Raija H., Taniguchi, Naoyuki, Taniguchi, Naoyuki, Teixeira, Felipe C.O.B., Teixeira, Felipe C.O.B., Tenni, Ruggero, Tenni, Ruggero, Tenni, Ruggero. Theocharis, Achilleas D., Theocharis, Achilleas D., Theocharis, Achilleas, Theocharis, Achilleas, Theocharis, Achilleas. Thidemann Johansen, Harald, Thidemann Johansen, Harald, Toriseva, Mervi, Toriseva, Mervi, Triantaphyllidou, Irene-Eva, Triantaphyllidou, Irene-Eva, Tsegenidis, Theodore, Tsegenidis, Theodore, Tzanakakis, George N., Tzanakakis, George N., Uhlin-Hansen, Lars, Uhlin-Hansen, Lars, Velasco, Jennifer, Velasco, Jennifer, Vigetti, Davide, Vigetti, Davide, Viola, Manuela, Viola, Manuela, Vlodavsky, Israel, Vlodavsky, Israel, Vynios, Demitrios H., Vynios, Demitrios H., Wang, Vincent, Wang, Vincent, Whiteford, James R., Whiteford, James R., Wight, Thomas N., Wight, Thomas N., Willis, Chris D., Willis, Chris D., Winberg, Jan-Olof, Winberg, Jan-Olof, Winberg, Jan-Olof. Xian, Xiaojie, Xian, Xiaojie, Zaman, Muhammad H., Zaman, Muhammad H., Zong, Fang, Zong, Fang, |
author_facet |
Afratis, Nikos, Afratis, Nikos, Aletras, Alexios J., Aletras, Alexios J., Bell, Rebecca, Bell, Rebecca, Bendeck, Michelle P., Bendeck, Michelle P., Berdiaki, Aikaterini, Berdiaki, Aikaterini, Boudko, Sergei P., Boudko, Sergei P., Bouga, Helen, Bouga, Helen, Brakebusch, Cord, Brakebusch, Cord, Brodsky, Barbara, Brodsky, Barbara, Bächinger, Hans Peter, Bächinger, Hans Peter, Capurro, Mariana, Capurro, Mariana, Casu, Benito, Casu, Benito, Couchman, John R., Couchman, John R., Dagälv, Anders, Dagälv, Anders, De Luca, Giancarlo, De Luca, Giancarlo, Deligny, Audrey, Deligny, Audrey, Des Parkin, J., Des Parkin, J., Do, Anh-Tri, Do, Anh-Tri, Dobra, Katalin, Dobra, Katalin, Dufour, Antoine, Dufour, Antoine, Elkin, Michael, Elkin, Michael, Fadnes, Bodil, Fadnes, Bodil, Filmus, Jorge, Filmus, Jorge, Filou, Serafoula, Filou, Serafoula, Gabison, Eric E, Gabison, Eric E, Gao, Congxiao, Gao, Congxiao, Ghatak, Shibnath, Ghatak, Shibnath, Gialeli, Chrisostomi, Gialeli, Chrisostomi, Gorski, Daniel J., Gorski, Daniel J., Gu, Jianguo, Gu, Jianguo, Gullberg, Donald, Gullberg, Donald, Gullberg, Donald. Hadler-Olsen, Elin, Hadler-Olsen, Elin, Hascall, Vincent C., Hascall, Vincent C., Hascall, Vincent, Hascall, Vincent, Heinegård, Dick, Heinegård, Dick, Heldin, Paraskevi, Heldin, Paraskevi, Hinz, Boris, Hinz, Boris, Hjerpe, Anders, Hjerpe, Anders, Huet, Eric, Huet, Eric, Hulmes, David J. S., Hulmes, David J. S., Ilan, Neta, Ilan, Neta, Iozzo, Renato V., Iozzo, Renato V., Jacenko, Olena, Jacenko, Olena, Jokela, Tiina A., Jokela, Tiina A., Karamanos, Nikos K., Karamanos, Nikos K., Karamanos, Nikos, Karamanos, Nikos, Karousou, Evgenia, Karousou, Evgenia, Kjelle, Lena, Kjelle, Lena, Kletsas, Dimitris, Kletsas, Dimitris, Kolliopoulos, Constantine, Kolliopoulos, Constantine, Korpetinou, Angeliki, Korpetinou, Angeliki, Koutsioumpa, Marina, Koutsioumpa, Marina, Kovalszky, Ilona, Kovalszky, Ilona, Kozlowski, Eliene O., Kozlowski, Eliene O., Kähäri, Veli-Matti, Kähäri, Veli-Matti, Labropoulou, Vassiliki, Labropoulou, Vassiliki, Li, Jin-Ping, Li, Jin-Ping, Lu, Ning, Lu, Ning, Maffei, Joseph S., Maffei, Joseph S., Magnussen, Synnøve, Magnussen, Synnøve, Markwald, Roger R., Markwald, Roger R., McCulloch, Christopher A., McCulloch, Christopher A., McNicols, Colton, McNicols, Colton, Menashi, Suzanne, Menashi, Suzanne, Merline, Rosetta, Merline, Rosetta, Milia-Argeiti, Eleni, Milia-Argeiti, Eleni, Misra, Suniti, Misra, Suniti, Mizumoto, Shuji, Mizumoto, Shuji, Moali, Catherine, Moali, Catherine, Mourah, Samia, Mourah, Samia, Nagase, Hideaki, Nagase, Hideaki, Nastase, Madalina V., Nastase, Madalina V., Nikitovic, Dragana, Nikitovic, Dragana, Ohtsubo, Kazuaki, Ohtsubo, Kazuaki, Oikari, Sanna, Oikari, Sanna, Orgel, Joseph P. R. O., Orgel, Joseph P. R. O., Overall, Christopher M., Overall, Christopher M., Papadimitriou, Evangelia, Papadimitriou, Evangelia, Paraskevi, Heldin. Passi, Alberto, Passi, Alberto, Pataki, Csilla, Pataki, Csilla, Pavao, Mauro S. G., Pavao, Mauro S. G., Persikov, Anton V., Persikov, Anton V., Pikas, Dagmar S., Pikas, Dagmar S., Plaas, Anna, Plaas, Anna, Pratsinis, Harris, Pratsinis, Harris, Pucci-Minafra, Ida, Pucci-Minafra, Ida, Puré, Ellen, Puré, Ellen, Raspanti, Mario, Raspanti, Mario, Rocca, Antonio S., Rocca, Antonio S., Rydén, Cecilia, Rydén, Cecilia, San Antonio, James D., San Antonio, James D., Sanderson, Ralph D., Sanderson, Ralph D., Sandy, John, Sandy, John, Sasaki, Takako, Sasaki, Takako, Savige, Judy, Savige, Judy, Schaefer, Liliana, Schaefer, Liliana, Schaefer, Liliana. Schick, Barbara P., Schick, Barbara P., Skandalis, Spyros S., Skandalis, Spyros S., Solberg, Rigmor, Solberg, Rigmor, Sugahara, Kazuyuki, Sugahara, Kazuyuki, Svineng, Gunbjørg, Svineng, Gunbjørg, Sylte, Ingebrigt, Sylte, Ingebrigt, Tammi, Markku I., Tammi, Markku I., Tammi, Raija H., Tammi, Raija H., Taniguchi, Naoyuki, Taniguchi, Naoyuki, Teixeira, Felipe C.O.B., Teixeira, Felipe C.O.B., Tenni, Ruggero, Tenni, Ruggero, Tenni, Ruggero. Theocharis, Achilleas D., Theocharis, Achilleas D., Theocharis, Achilleas, Theocharis, Achilleas, Theocharis, Achilleas. Thidemann Johansen, Harald, Thidemann Johansen, Harald, Toriseva, Mervi, Toriseva, Mervi, Triantaphyllidou, Irene-Eva, Triantaphyllidou, Irene-Eva, Tsegenidis, Theodore, Tsegenidis, Theodore, Tzanakakis, George N., Tzanakakis, George N., Uhlin-Hansen, Lars, Uhlin-Hansen, Lars, Velasco, Jennifer, Velasco, Jennifer, Vigetti, Davide, Vigetti, Davide, Viola, Manuela, Viola, Manuela, Vlodavsky, Israel, Vlodavsky, Israel, Vynios, Demitrios H., Vynios, Demitrios H., Wang, Vincent, Wang, Vincent, Whiteford, James R., Whiteford, James R., Wight, Thomas N., Wight, Thomas N., Willis, Chris D., Willis, Chris D., Winberg, Jan-Olof, Winberg, Jan-Olof, Winberg, Jan-Olof. Xian, Xiaojie, Xian, Xiaojie, Zaman, Muhammad H., Zaman, Muhammad H., Zong, Fang, Zong, Fang, |
author2_variant |
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author2_role |
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author_sort |
Afratis, Nikos, |
title |
Extracellular Matrix: Pathobiology and Signaling / |
spellingShingle |
Extracellular Matrix: Pathobiology and Signaling / Frontmatter -- Contents -- Preface -- Comments on the book Extracellular Matrix: Pathobiology & Signaling -- About the Editor/Section Editors -- List of contributing authors -- Abbreviations and acronyms used -- 1 An introduction to the extracellular matrix molecules and their importance in pathobiology and signaling -- 1.1 Extracellular matrix: a functional scaffold -- 2 Insights into the function of glycans -- 2.1 Introduction -- 2.2 Metabolic control of hyaluronan synthesis -- 2.3 Multiple roles of hyaluronan as a target and modifier of the inflammatory response -- 2.4 Roles of sulfated and nonsulfated glycosaminoglycans in cancer growth and progression-therapeutic implications -- 2.5 Heparan sulfate design: regulation of biosynthesis -- 2.6 Bone and skin disorders caused by a disturbance in the biosynthesis of chondroitin sulfate and dermatan sulfate -- 2.7 Biological functions of branched N-glycans related to physiology and pathology of extracellular matrix -- 3 Proteoglycans: structure, pathobiology, and signaling -- 3.1 Introduction -- 3.2 Aggrecan in skeletal development and regenerative medicine -- 3.3 The pathobiology of versican -- 3.4 The biology of perlecan and its bioactive modules -- 3.5 Small leucine-rich proteoglycans: multifunctional signaling effectors -- 3.6 Structure and function of syndecans -- 3.7 The glypican family -- 3.8 Serglycin proteoglycan: implications for thrombosis, inflammation, atherosclerosis, and metastasis -- 4 Matrix Proteinases: biological significance in health and disease -- 4.1 Introduction -- 4.2 Extracellular functions of cysteine proteases -- 4.3 Plasmin and the plasminogen activator system in health and disease -- 4.4 Matrix metalloproteinase complexes and their biological significance -- 4.5 The ADAMTS family of metalloproteinases -- 4.6 Proteinases in wound healing -- 4.7 Rock, paper, and molecular scissors: regulating the game of extracellular matrix homeostasis, remodeling, and inflammation -- 5 ECM cell surface receptors -- 5.1 Introduction -- 5.2 Integrin function in heart fibrosis: mechanical strain, transforming growth factor-beta 1 activation, and collagen glycation -- 5.3 Cancer-associated fibroblast integrins as therapeutic targets in the tumor microenvironment -- 5.4 Discoidin domain receptors: non-integrin collagen receptors on the move -- 5.5 Syndecans as receptors for pericellular molecules -- 5.6 CD44: a Sensor of tissue damage critical for restoring homeostasis -- 6 Collagens: insights into the folding, assembly and functions -- 6.1 Introduction -- 6.2 Trimerization domains in collagens: chain selection, folding initiation, and triple-helix stabilization -- 6.3 Structural basis of collagen missense mutations -- 6.4 Roles and regulation of BMP1/Tolloid-like proteinases: collagen/matrix assembly, growth factor activation, and beyond -- 6.5 Supramolecular assembly of type I collagen -- 6.6 Collagen interactomes: mapping functional domains and mutations on fibrillar and network-forming collagens -- 6.7 Collagen-binding proteins -- 7 Emerging aspects in extracellular matrix pathobiology -- 7.1 Introduction -- 7.2 Extracellular matrix in breast cancer: permissive and restrictive influences emanating from the stroma -- 7.3 EMMPRIN/CD147: potential functions in tumor microenvironment and therapeutic target for human cancer -- 7.4 Implication of hyaluronidases in cancer growth, metastasis, diagnosis, and treatment -- 7.5 Structure-function relationship of syndecan-1, with focus on nuclear translocation and tumor cell behavior -- 7.6 Serglycin: a novel player in the terrain of neoplasia -- 7.7 Quantifying cell-ECM pathobiology in 3D -- 7.8 Diabetic foot infections -- 8 Targeting tumor microenvironment at the ECM level -- 8.1 Introduction -- 8.2 Targeting the tumor microenvironment in cancer progression -- 8.3 Growth factor signaling and extracellular matrix -- 8.4 Targeting protein-glycan interactions at cell surface during EMT and hematogenous metastasis: consequences on tumor invasion and metastasis -- 8.5 Pharmacological targeting of proteoglycans and metalloproteinases: an emerging aspect in cancer treatment -- 8.6 Targeting syndecan shedding in cancer -- 8.7 PG receptors with phosphatase action in cancer and angiogenesis -- 8.8 Heparanase, a multifaceted protein involved in cancer, chronic inflammation, and kidney dysfunction -- 8.9 Delivery systems targeting cancer at the level of ECM -- Index |
title_full |
Extracellular Matrix: Pathobiology and Signaling / ed. by Nikos Karamanos. |
title_fullStr |
Extracellular Matrix: Pathobiology and Signaling / ed. by Nikos Karamanos. |
title_full_unstemmed |
Extracellular Matrix: Pathobiology and Signaling / ed. by Nikos Karamanos. |
title_auth |
Extracellular Matrix: Pathobiology and Signaling / |
title_alt |
Frontmatter -- Contents -- Preface -- Comments on the book Extracellular Matrix: Pathobiology & Signaling -- About the Editor/Section Editors -- List of contributing authors -- Abbreviations and acronyms used -- 1 An introduction to the extracellular matrix molecules and their importance in pathobiology and signaling -- 1.1 Extracellular matrix: a functional scaffold -- 2 Insights into the function of glycans -- 2.1 Introduction -- 2.2 Metabolic control of hyaluronan synthesis -- 2.3 Multiple roles of hyaluronan as a target and modifier of the inflammatory response -- 2.4 Roles of sulfated and nonsulfated glycosaminoglycans in cancer growth and progression-therapeutic implications -- 2.5 Heparan sulfate design: regulation of biosynthesis -- 2.6 Bone and skin disorders caused by a disturbance in the biosynthesis of chondroitin sulfate and dermatan sulfate -- 2.7 Biological functions of branched N-glycans related to physiology and pathology of extracellular matrix -- 3 Proteoglycans: structure, pathobiology, and signaling -- 3.1 Introduction -- 3.2 Aggrecan in skeletal development and regenerative medicine -- 3.3 The pathobiology of versican -- 3.4 The biology of perlecan and its bioactive modules -- 3.5 Small leucine-rich proteoglycans: multifunctional signaling effectors -- 3.6 Structure and function of syndecans -- 3.7 The glypican family -- 3.8 Serglycin proteoglycan: implications for thrombosis, inflammation, atherosclerosis, and metastasis -- 4 Matrix Proteinases: biological significance in health and disease -- 4.1 Introduction -- 4.2 Extracellular functions of cysteine proteases -- 4.3 Plasmin and the plasminogen activator system in health and disease -- 4.4 Matrix metalloproteinase complexes and their biological significance -- 4.5 The ADAMTS family of metalloproteinases -- 4.6 Proteinases in wound healing -- 4.7 Rock, paper, and molecular scissors: regulating the game of extracellular matrix homeostasis, remodeling, and inflammation -- 5 ECM cell surface receptors -- 5.1 Introduction -- 5.2 Integrin function in heart fibrosis: mechanical strain, transforming growth factor-beta 1 activation, and collagen glycation -- 5.3 Cancer-associated fibroblast integrins as therapeutic targets in the tumor microenvironment -- 5.4 Discoidin domain receptors: non-integrin collagen receptors on the move -- 5.5 Syndecans as receptors for pericellular molecules -- 5.6 CD44: a Sensor of tissue damage critical for restoring homeostasis -- 6 Collagens: insights into the folding, assembly and functions -- 6.1 Introduction -- 6.2 Trimerization domains in collagens: chain selection, folding initiation, and triple-helix stabilization -- 6.3 Structural basis of collagen missense mutations -- 6.4 Roles and regulation of BMP1/Tolloid-like proteinases: collagen/matrix assembly, growth factor activation, and beyond -- 6.5 Supramolecular assembly of type I collagen -- 6.6 Collagen interactomes: mapping functional domains and mutations on fibrillar and network-forming collagens -- 6.7 Collagen-binding proteins -- 7 Emerging aspects in extracellular matrix pathobiology -- 7.1 Introduction -- 7.2 Extracellular matrix in breast cancer: permissive and restrictive influences emanating from the stroma -- 7.3 EMMPRIN/CD147: potential functions in tumor microenvironment and therapeutic target for human cancer -- 7.4 Implication of hyaluronidases in cancer growth, metastasis, diagnosis, and treatment -- 7.5 Structure-function relationship of syndecan-1, with focus on nuclear translocation and tumor cell behavior -- 7.6 Serglycin: a novel player in the terrain of neoplasia -- 7.7 Quantifying cell-ECM pathobiology in 3D -- 7.8 Diabetic foot infections -- 8 Targeting tumor microenvironment at the ECM level -- 8.1 Introduction -- 8.2 Targeting the tumor microenvironment in cancer progression -- 8.3 Growth factor signaling and extracellular matrix -- 8.4 Targeting protein-glycan interactions at cell surface during EMT and hematogenous metastasis: consequences on tumor invasion and metastasis -- 8.5 Pharmacological targeting of proteoglycans and metalloproteinases: an emerging aspect in cancer treatment -- 8.6 Targeting syndecan shedding in cancer -- 8.7 PG receptors with phosphatase action in cancer and angiogenesis -- 8.8 Heparanase, a multifaceted protein involved in cancer, chronic inflammation, and kidney dysfunction -- 8.9 Delivery systems targeting cancer at the level of ECM -- Index |
title_new |
Extracellular Matrix: Pathobiology and Signaling / |
title_sort |
extracellular matrix: pathobiology and signaling / |
publisher |
De Gruyter, |
publishDate |
2012 |
physical |
1 online resource (888 p.) |
contents |
Frontmatter -- Contents -- Preface -- Comments on the book Extracellular Matrix: Pathobiology & Signaling -- About the Editor/Section Editors -- List of contributing authors -- Abbreviations and acronyms used -- 1 An introduction to the extracellular matrix molecules and their importance in pathobiology and signaling -- 1.1 Extracellular matrix: a functional scaffold -- 2 Insights into the function of glycans -- 2.1 Introduction -- 2.2 Metabolic control of hyaluronan synthesis -- 2.3 Multiple roles of hyaluronan as a target and modifier of the inflammatory response -- 2.4 Roles of sulfated and nonsulfated glycosaminoglycans in cancer growth and progression-therapeutic implications -- 2.5 Heparan sulfate design: regulation of biosynthesis -- 2.6 Bone and skin disorders caused by a disturbance in the biosynthesis of chondroitin sulfate and dermatan sulfate -- 2.7 Biological functions of branched N-glycans related to physiology and pathology of extracellular matrix -- 3 Proteoglycans: structure, pathobiology, and signaling -- 3.1 Introduction -- 3.2 Aggrecan in skeletal development and regenerative medicine -- 3.3 The pathobiology of versican -- 3.4 The biology of perlecan and its bioactive modules -- 3.5 Small leucine-rich proteoglycans: multifunctional signaling effectors -- 3.6 Structure and function of syndecans -- 3.7 The glypican family -- 3.8 Serglycin proteoglycan: implications for thrombosis, inflammation, atherosclerosis, and metastasis -- 4 Matrix Proteinases: biological significance in health and disease -- 4.1 Introduction -- 4.2 Extracellular functions of cysteine proteases -- 4.3 Plasmin and the plasminogen activator system in health and disease -- 4.4 Matrix metalloproteinase complexes and their biological significance -- 4.5 The ADAMTS family of metalloproteinases -- 4.6 Proteinases in wound healing -- 4.7 Rock, paper, and molecular scissors: regulating the game of extracellular matrix homeostasis, remodeling, and inflammation -- 5 ECM cell surface receptors -- 5.1 Introduction -- 5.2 Integrin function in heart fibrosis: mechanical strain, transforming growth factor-beta 1 activation, and collagen glycation -- 5.3 Cancer-associated fibroblast integrins as therapeutic targets in the tumor microenvironment -- 5.4 Discoidin domain receptors: non-integrin collagen receptors on the move -- 5.5 Syndecans as receptors for pericellular molecules -- 5.6 CD44: a Sensor of tissue damage critical for restoring homeostasis -- 6 Collagens: insights into the folding, assembly and functions -- 6.1 Introduction -- 6.2 Trimerization domains in collagens: chain selection, folding initiation, and triple-helix stabilization -- 6.3 Structural basis of collagen missense mutations -- 6.4 Roles and regulation of BMP1/Tolloid-like proteinases: collagen/matrix assembly, growth factor activation, and beyond -- 6.5 Supramolecular assembly of type I collagen -- 6.6 Collagen interactomes: mapping functional domains and mutations on fibrillar and network-forming collagens -- 6.7 Collagen-binding proteins -- 7 Emerging aspects in extracellular matrix pathobiology -- 7.1 Introduction -- 7.2 Extracellular matrix in breast cancer: permissive and restrictive influences emanating from the stroma -- 7.3 EMMPRIN/CD147: potential functions in tumor microenvironment and therapeutic target for human cancer -- 7.4 Implication of hyaluronidases in cancer growth, metastasis, diagnosis, and treatment -- 7.5 Structure-function relationship of syndecan-1, with focus on nuclear translocation and tumor cell behavior -- 7.6 Serglycin: a novel player in the terrain of neoplasia -- 7.7 Quantifying cell-ECM pathobiology in 3D -- 7.8 Diabetic foot infections -- 8 Targeting tumor microenvironment at the ECM level -- 8.1 Introduction -- 8.2 Targeting the tumor microenvironment in cancer progression -- 8.3 Growth factor signaling and extracellular matrix -- 8.4 Targeting protein-glycan interactions at cell surface during EMT and hematogenous metastasis: consequences on tumor invasion and metastasis -- 8.5 Pharmacological targeting of proteoglycans and metalloproteinases: an emerging aspect in cancer treatment -- 8.6 Targeting syndecan shedding in cancer -- 8.7 PG receptors with phosphatase action in cancer and angiogenesis -- 8.8 Heparanase, a multifaceted protein involved in cancer, chronic inflammation, and kidney dysfunction -- 8.9 Delivery systems targeting cancer at the level of ECM -- Index |
isbn |
9783110258776 9783110238570 9783110238495 9783110637915 9783110288995 9783110294071 9783110294064 9783110258769 |
callnumber-first |
Q - Science |
callnumber-subject |
QP - Physiology |
callnumber-label |
QP88 |
callnumber-sort |
QP 288.23 E98 42012 |
url |
https://doi.org/10.1515/9783110258776 https://www.degruyter.com/isbn/9783110258776 https://www.degruyter.com/cover/covers/9783110258776.jpg |
illustrated |
Not Illustrated |
dewey-hundreds |
600 - Technology |
dewey-tens |
610 - Medicine & health |
dewey-ones |
610 - Medicine & health |
dewey-full |
610 |
dewey-sort |
3610 |
dewey-raw |
610 |
dewey-search |
610 |
doi_str_mv |
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Title is part of eBook package: De Gruyter DGBA Backlist Complete English Language 2000-2014 PART1 Title is part of eBook package: De Gruyter DGBA Backlist Medicine and Life Sciences 2000-2014 (EN) Title is part of eBook package: De Gruyter DGBA Medicine and Life Sciences 2000 - 2014 Title is part of eBook package: De Gruyter E-BOOK GESAMTPAKET / COMPLETE PACKAGE 2012 Title is part of eBook package: De Gruyter E-BOOK PACKAGE BIOLOGY, CHEMISTRY, GEOSCIENCES 2012 Title is part of eBook package: De Gruyter E-BOOK PAKET BIOLOGIE, CHEMIE, GEOWISS. 2012 |
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Extracellular Matrix: Pathobiology and Signaling / |
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branched N-glycans related to physiology and pathology of extracellular matrix -- </subfield><subfield code="t">3 Proteoglycans: structure, pathobiology, and signaling -- </subfield><subfield code="t">3.1 Introduction -- </subfield><subfield code="t">3.2 Aggrecan in skeletal development and regenerative medicine -- </subfield><subfield code="t">3.3 The pathobiology of versican -- </subfield><subfield code="t">3.4 The biology of perlecan and its bioactive modules -- </subfield><subfield code="t">3.5 Small leucine-rich proteoglycans: multifunctional signaling effectors -- </subfield><subfield code="t">3.6 Structure and function of syndecans -- </subfield><subfield code="t">3.7 The glypican family -- </subfield><subfield code="t">3.8 Serglycin proteoglycan: implications for thrombosis, inflammation, atherosclerosis, and metastasis -- </subfield><subfield code="t">4 Matrix Proteinases: biological significance in health and disease -- </subfield><subfield code="t">4.1 Introduction -- </subfield><subfield code="t">4.2 Extracellular functions of cysteine proteases -- </subfield><subfield code="t">4.3 Plasmin and the plasminogen activator system in health and disease -- </subfield><subfield code="t">4.4 Matrix metalloproteinase complexes and their biological significance -- </subfield><subfield code="t">4.5 The ADAMTS family of metalloproteinases -- </subfield><subfield code="t">4.6 Proteinases in wound healing -- </subfield><subfield code="t">4.7 Rock, paper, and molecular scissors: regulating the game of extracellular matrix homeostasis, remodeling, and inflammation -- </subfield><subfield code="t">5 ECM cell surface receptors -- </subfield><subfield code="t">5.1 Introduction -- </subfield><subfield code="t">5.2 Integrin function in heart fibrosis: mechanical strain, transforming growth factor-beta 1 activation, and collagen glycation -- </subfield><subfield code="t">5.3 Cancer-associated fibroblast integrins as therapeutic targets in the tumor microenvironment -- </subfield><subfield code="t">5.4 Discoidin domain receptors: non-integrin collagen receptors on the move -- </subfield><subfield code="t">5.5 Syndecans as receptors for pericellular molecules -- </subfield><subfield code="t">5.6 CD44: a Sensor of tissue damage critical for restoring homeostasis -- </subfield><subfield code="t">6 Collagens: insights into the folding, assembly and functions -- </subfield><subfield code="t">6.1 Introduction -- </subfield><subfield code="t">6.2 Trimerization domains in collagens: chain selection, folding initiation, and triple-helix stabilization -- </subfield><subfield code="t">6.3 Structural basis of collagen missense mutations -- </subfield><subfield code="t">6.4 Roles and regulation of BMP1/Tolloid-like proteinases: collagen/matrix assembly, growth factor activation, and beyond -- </subfield><subfield code="t">6.5 Supramolecular assembly of type I collagen -- </subfield><subfield code="t">6.6 Collagen interactomes: mapping functional domains and mutations on fibrillar and network-forming collagens -- </subfield><subfield code="t">6.7 Collagen-binding proteins -- </subfield><subfield code="t">7 Emerging aspects in extracellular matrix pathobiology -- </subfield><subfield code="t">7.1 Introduction -- </subfield><subfield code="t">7.2 Extracellular matrix in breast cancer: permissive and restrictive influences emanating from the stroma -- </subfield><subfield code="t">7.3 EMMPRIN/CD147: potential functions in tumor microenvironment and therapeutic target for human cancer -- </subfield><subfield code="t">7.4 Implication of hyaluronidases in cancer growth, metastasis, diagnosis, and treatment -- </subfield><subfield code="t">7.5 Structure-function relationship of syndecan-1, with focus on nuclear translocation and tumor cell behavior -- </subfield><subfield code="t">7.6 Serglycin: a novel player in the terrain of neoplasia -- </subfield><subfield code="t">7.7 Quantifying cell-ECM pathobiology in 3D -- </subfield><subfield code="t">7.8 Diabetic foot infections -- </subfield><subfield code="t">8 Targeting tumor microenvironment at the ECM level -- </subfield><subfield code="t">8.1 Introduction -- </subfield><subfield code="t">8.2 Targeting the tumor microenvironment in cancer progression -- </subfield><subfield code="t">8.3 Growth factor signaling and extracellular matrix -- </subfield><subfield code="t">8.4 Targeting protein-glycan interactions at cell surface during EMT and hematogenous metastasis: consequences on tumor invasion and metastasis -- </subfield><subfield code="t">8.5 Pharmacological targeting of proteoglycans and metalloproteinases: an emerging aspect in cancer treatment -- </subfield><subfield code="t">8.6 Targeting syndecan shedding in cancer -- </subfield><subfield code="t">8.7 PG receptors with phosphatase action in cancer and angiogenesis -- </subfield><subfield code="t">8.8 Heparanase, a multifaceted protein involved in cancer, chronic inflammation, and kidney dysfunction -- </subfield><subfield code="t">8.9 Delivery systems targeting cancer at the level of ECM -- </subfield><subfield code="t">Index</subfield></datafield><datafield tag="506" ind1="0" ind2=" "><subfield code="a">restricted access</subfield><subfield code="u">http://purl.org/coar/access_right/c_16ec</subfield><subfield code="f">online access with authorization</subfield><subfield code="2">star</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Over the last decades cell biology and biological chemistry have increasingly turned their attention to the space between cells and revealed an elaborate network of macromolecules essential for structural support, cell adhesion and signaling. This comprehensive handbook of the extracellular matrix will give an overview of the current state of knowledge of matrix components (structure and function), their role in heath and disease (matrix pathobiology) and new aspects related to pharmacological targeting.It will provide an introduction to the extracellular matrix and detailed sections and chapters on: Importance of extracellular matrix in health and disease Matrix proteoglycans (aggrecan, versican, perlecan, SLRPs, syndecans, glypicans, serglycin) Matrix proteinases (remodeling, would healing, regulatory roles in health and disease, metalloproteinases, cystein proteases, plasmin and plasminogen activator system) Glycobiology (hyaluronan and sulfated glycosaminoglycans in cancer, inflammation and metabolic control) Collagens (supramolecular assembly, proteins binding collagen, scaffolds, bacterial and mutated collagens, procollagen proteinases) Cell surface receptors (integrins, syndecans, mechanical strain and TGFb, CD44 and DDR). Biotechnological and pharmacological outlook (matrix regulation by growth factors, hyaluronidases, pathobiology, disease targeting, delivery systems, EMT and proteomics). "The book Extracellular Matrix: Pathobiology and Signaling provides a comprehensive and up to date collection of very relevant topics for understanding the various facets of extracellular matrix and its interactions with cells in normal tissue as well as in disease. It represents the current front-line and will serve as a reference for extracellular matrix and posttranslational modifications." Dick Heinegård, Department of Clinical Sciences Lund, Section Rheumatology, Lund University, Sweden</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Over the last decades cell biology and biological chemistry have increasingly turned their attention to the space between cells and revealed an elaborate network of macromolecules essential for structural support, cell migration, adhesion and signaling. This comprehensive handbook of the extracellular matrix is organized into seven thematic sections, giving an overview of the current state of knowledge of matrix components (structure and function), their roles in health and disease (matrix pathobiology) as well as new concepts of pharmacological targeting.</subfield></datafield><datafield tag="538" ind1=" " ind2=" "><subfield code="a">Mode of access: Internet via World Wide Web.</subfield></datafield><datafield tag="546" ind1=" " ind2=" "><subfield code="a">In English.</subfield></datafield><datafield tag="588" ind1="0" ind2=" "><subfield code="a">Description based on online resource; title from PDF title page (publisher's Web site, viewed 30. Aug 2021)</subfield></datafield><datafield tag="650" ind1=" " ind2="0"><subfield code="a">Cellular signal transduction.</subfield></datafield><datafield tag="650" ind1=" " ind2="0"><subfield code="a">Extracellular matrix</subfield><subfield code="x">Pathophysiology.</subfield></datafield><datafield tag="650" ind1=" " ind2="0"><subfield code="a">Extracellular matrix</subfield><subfield code="x">Physiology.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Biochemie.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Glykane.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Kollagene.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Matrix.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Metalloproteinasen.</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">SCIENCE / Life Sciences / 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