TGF- and Related Cytokines in Inflammation Progress in Inflammation Research
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1
TGF-ss and Related Cytokines in Inflammation
DE PB NW
ISBN: 9783034895316 bzw. 3034895313, in Deutsch, Birkhäuser, Taschenbuch, neu.
Lieferung aus: Deutschland, Versandkostenfrei.
buecher.de GmbH & Co. KG, [1].
This book is a comprehensive review of the structure/function and biology of molecules belonging to the TGF-ss superfamily. Because molecules in this family have very diverse biological roles the editors have chosen to focus on the parts they play in the specific areas of inflammation and wound/fracture healing.Whilst molecules in the TGF-ss superfamily have been extensively studied, there are few, if any, publications which have taken a broad perspective on this family, most having chosen to focus on just one very small area.This book is therefore unusual in that it offers a comprehensive overview of the current state of the field, providing both in-depth and essential background material suitable for both clinicians and scientists alike.Softcover reprint of the original 1st ed. 2001. 2012. xiii, 202 S. XIII, 202 p. 235 mmVersandfertig in 3-5 Tagen, Softcover.
buecher.de GmbH & Co. KG, [1].
This book is a comprehensive review of the structure/function and biology of molecules belonging to the TGF-ss superfamily. Because molecules in this family have very diverse biological roles the editors have chosen to focus on the parts they play in the specific areas of inflammation and wound/fracture healing.Whilst molecules in the TGF-ss superfamily have been extensively studied, there are few, if any, publications which have taken a broad perspective on this family, most having chosen to focus on just one very small area.This book is therefore unusual in that it offers a comprehensive overview of the current state of the field, providing both in-depth and essential background material suitable for both clinicians and scientists alike.Softcover reprint of the original 1st ed. 2001. 2012. xiii, 202 S. XIII, 202 p. 235 mmVersandfertig in 3-5 Tagen, Softcover.
2
Symbolbild
TGF- and Related Cytokines in Inflammation Progress in Inflammation Research
DE PB NW
ISBN: 9783034895316 bzw. 3034895313, in Deutsch, Birkhäuser, Taschenbuch, neu.
Von Händler/Antiquariat, BuySomeBooks [52360437], Las Vegas, NV, U.S.A.
Paperback. 202 pages. Dimensions: 9.2in. x 6.1in. x 0.5in.The TGF-13 superfamily is a large and expanding multigene family which in verte brates includes the TGF-13 proteins themselves, the bone morphogenetic proteins (BMPs), the growth and differentiation factors (GDF), the activinsinhibins (INH), Mullerian inhibitory substance (MIS), glial derived neurotropic factor (GDNF) and more recently macrophage inhibitory cytokine 1 (MIC-1). They are characterised by conserved structural elements and a broad commonality of function. Major structural elements All members of the TGF-13 superfamily contain as their major structural hallmark a conserved spacing and distribution of seven cysteine residues. This structure is known as the cysteine knot and tethers together regions of the peptide as well as binding the two chains of the dimer to each other. High resolution structures are now available on proteins from three families within this group including glial derived neurotropic factor (GDNF), BMP-7 and several of the TGF-13s. Despite low similarity between some of these proteins (eg, TGF-13s and GDNF are only 13 identical) they share a strikingly similar three dimensional conformation (Fig. 1). These structural elements imbue the protein with some of its familial characteristics. These include its physico-chemical stability due to tight tethering of portions of the peptide chain via criss-crossing disulphide bonds. Much of its surfaces are coated with hydrophobic patches leading to a propensity to bind non-specifically to other proteins as well as to its self. This also causes a marked propensity for aggregation when the recombinant protein is present at high concentration. This item ships from multiple locations. Your book may arrive from Roseburg,OR, La Vergne,TN.
Paperback. 202 pages. Dimensions: 9.2in. x 6.1in. x 0.5in.The TGF-13 superfamily is a large and expanding multigene family which in verte brates includes the TGF-13 proteins themselves, the bone morphogenetic proteins (BMPs), the growth and differentiation factors (GDF), the activinsinhibins (INH), Mullerian inhibitory substance (MIS), glial derived neurotropic factor (GDNF) and more recently macrophage inhibitory cytokine 1 (MIC-1). They are characterised by conserved structural elements and a broad commonality of function. Major structural elements All members of the TGF-13 superfamily contain as their major structural hallmark a conserved spacing and distribution of seven cysteine residues. This structure is known as the cysteine knot and tethers together regions of the peptide as well as binding the two chains of the dimer to each other. High resolution structures are now available on proteins from three families within this group including glial derived neurotropic factor (GDNF), BMP-7 and several of the TGF-13s. Despite low similarity between some of these proteins (eg, TGF-13s and GDNF are only 13 identical) they share a strikingly similar three dimensional conformation (Fig. 1). These structural elements imbue the protein with some of its familial characteristics. These include its physico-chemical stability due to tight tethering of portions of the peptide chain via criss-crossing disulphide bonds. Much of its surfaces are coated with hydrophobic patches leading to a propensity to bind non-specifically to other proteins as well as to its self. This also causes a marked propensity for aggregation when the recombinant protein is present at high concentration. This item ships from multiple locations. Your book may arrive from Roseburg,OR, La Vergne,TN.
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TGF-SS and Related Cytokines in Inflammation (Paperback) (2012)
DE PB NW RP
ISBN: 9783034895316 bzw. 3034895313, in Deutsch, Springer Basel, Switzerland, Taschenbuch, neu, Nachdruck.
Von Händler/Antiquariat, The Book Depository EURO [60485773], London, United Kingdom.
Language: English Brand New Book ***** Print on Demand *****.The TGF-13 superfamily is a large and expanding multigene family which in verte- brates includes the TGF-13 proteins themselves, the bone morphogenetic proteins (BMPs), the growth and differentiation factors (GDF), the activins/inhibins (INH), Mullerian inhibitory substance (MIS), glial derived neurotropic factor (GDNF) and more recently macrophage inhibitory cytokine 1 (MIC-1). They are characterised by conserved structural elements and a broad commonality of function. Major structural elements All members of the TGF-13 superfamily contain as their major structural hallmark a conserved spacing and distribution of seven cysteine residues. This structure is known as the cysteine knot and tethers together regions of the peptide as well as binding the two chains of the dimer to each other. High resolution structures are now available on proteins from three families within this group including glial derived neurotropic factor (GDNF), BMP-7 and several of the TGF-13s. Despite low similarity between some of these proteins (eg, TGF-13s and GDNF are only 13 identical) they share a strikingly similar three dimensional conformation (Fig. 1). These structural elements imbue the protein with some of its familial characteristics. These include its physico-chemical stability due to tight tethering of portions of the peptide chain via criss-crossing disulphide bonds. Much of its surfaces are coated with hydrophobic patches leading to a propensity to bind non-specifically to other proteins as well as to its self. This also causes a marked propensity for aggregation when the recombinant protein is present at high concentration. Softcover reprint of the original 1st ed. 2001.
Language: English Brand New Book ***** Print on Demand *****.The TGF-13 superfamily is a large and expanding multigene family which in verte- brates includes the TGF-13 proteins themselves, the bone morphogenetic proteins (BMPs), the growth and differentiation factors (GDF), the activins/inhibins (INH), Mullerian inhibitory substance (MIS), glial derived neurotropic factor (GDNF) and more recently macrophage inhibitory cytokine 1 (MIC-1). They are characterised by conserved structural elements and a broad commonality of function. Major structural elements All members of the TGF-13 superfamily contain as their major structural hallmark a conserved spacing and distribution of seven cysteine residues. This structure is known as the cysteine knot and tethers together regions of the peptide as well as binding the two chains of the dimer to each other. High resolution structures are now available on proteins from three families within this group including glial derived neurotropic factor (GDNF), BMP-7 and several of the TGF-13s. Despite low similarity between some of these proteins (eg, TGF-13s and GDNF are only 13 identical) they share a strikingly similar three dimensional conformation (Fig. 1). These structural elements imbue the protein with some of its familial characteristics. These include its physico-chemical stability due to tight tethering of portions of the peptide chain via criss-crossing disulphide bonds. Much of its surfaces are coated with hydrophobic patches leading to a propensity to bind non-specifically to other proteins as well as to its self. This also causes a marked propensity for aggregation when the recombinant protein is present at high concentration. Softcover reprint of the original 1st ed. 2001.
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Symbolbild
TGF-SS and Related Cytokines in Inflammation
EN NW
ISBN: 9783034895316 bzw. 3034895313, in Englisch, Springer Basel, neu.
Lieferung aus: Vereinigtes Königreich Grossbritannien und Nordirland, in-stock.
The TGF-13 superfamily is a large and expanding multigene family which in verte- brates includes the TGF-13 proteins themselves, the bone morphogenetic proteins (BMPs), the growth and differentiation factors (GDF), the activins/inhibins (INH), Mullerian inhibitory substance (MIS), glial derived neurotropic factor (GDNF) and more recently macrophage inhibitory cytokine 1 (MIC-1). They are characterised by conserved structural elements and a broad commonality of function. Major structural elements All members of the TGF-13 superfamily contain as their major structural hallmark a conserved spacing and distribution of seven cysteine residues. This structure is known as the cysteine knot and tethers together regions of the peptide as well as binding the two chains of the dimer to each other. High resolution structures are now available on proteins from three families within this group including glial derived neurotropic factor (GDNF), BMP-7 and several of the TGF-13s. Despite low similarity between some of these proteins (eg, TGF-13s and GDNF are only 13% identical) they share a strikingly similar three dimensional conformation (Fig. 1). These structural elements imbue the protein with some of its familial characteristics. These include its physico-chemical stability due to tight tethering of portions of the peptide chain via criss-crossing disulphide bonds. Much of its surfaces are coated with hydrophobic patches leading to a propensity to bind non-specifically to other proteins as well as to its self. This also causes a marked propensity for aggregation when the recombinant protein is present at high concentration.
The TGF-13 superfamily is a large and expanding multigene family which in verte- brates includes the TGF-13 proteins themselves, the bone morphogenetic proteins (BMPs), the growth and differentiation factors (GDF), the activins/inhibins (INH), Mullerian inhibitory substance (MIS), glial derived neurotropic factor (GDNF) and more recently macrophage inhibitory cytokine 1 (MIC-1). They are characterised by conserved structural elements and a broad commonality of function. Major structural elements All members of the TGF-13 superfamily contain as their major structural hallmark a conserved spacing and distribution of seven cysteine residues. This structure is known as the cysteine knot and tethers together regions of the peptide as well as binding the two chains of the dimer to each other. High resolution structures are now available on proteins from three families within this group including glial derived neurotropic factor (GDNF), BMP-7 and several of the TGF-13s. Despite low similarity between some of these proteins (eg, TGF-13s and GDNF are only 13% identical) they share a strikingly similar three dimensional conformation (Fig. 1). These structural elements imbue the protein with some of its familial characteristics. These include its physico-chemical stability due to tight tethering of portions of the peptide chain via criss-crossing disulphide bonds. Much of its surfaces are coated with hydrophobic patches leading to a propensity to bind non-specifically to other proteins as well as to its self. This also causes a marked propensity for aggregation when the recombinant protein is present at high concentration.
5
TGF-β and Related Cytokines in Inflammation (Progress in Inflammation Research) (2013)
EN NW FE EB DL
ISBN: 9783034883542 bzw. 3034883544, in Englisch, 201 Seiten, Birkhäuser, neu, Erstausgabe, E-Book, elektronischer Download.
Lieferung aus: Deutschland, E-Book zum Download, Versandkostenfrei.
This book is a comprehensive review of the structure/function and biology of molecules belonging to the TGF-ss superfamily. Because molecules in this family have very diverse biological roles the editors have chosen to focus on the parts they play in the specific areas of inflammation and wound/fracture healing. Whilst molecules in the TGF-ss superfamily have been extensively studied, there are few, if any, publications which have taken a broad perspective on this family, most having chosen to focus on just one very small area. This book is therefore unusual in that it offers a comprehensive overview of the current state of the field, providing both in-depth and essential background material suitable for both clinicians and scientists alike. Kindle Edition, Ausgabe: 1, Format: Kindle eBook, Label: Birkhäuser, Birkhäuser, Produktgruppe: eBooks, Publiziert: 2013-03-07, Freigegeben: 2013-03-07, Studio: Birkhäuser.
This book is a comprehensive review of the structure/function and biology of molecules belonging to the TGF-ss superfamily. Because molecules in this family have very diverse biological roles the editors have chosen to focus on the parts they play in the specific areas of inflammation and wound/fracture healing. Whilst molecules in the TGF-ss superfamily have been extensively studied, there are few, if any, publications which have taken a broad perspective on this family, most having chosen to focus on just one very small area. This book is therefore unusual in that it offers a comprehensive overview of the current state of the field, providing both in-depth and essential background material suitable for both clinicians and scientists alike. Kindle Edition, Ausgabe: 1, Format: Kindle eBook, Label: Birkhäuser, Birkhäuser, Produktgruppe: eBooks, Publiziert: 2013-03-07, Freigegeben: 2013-03-07, Studio: Birkhäuser.
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TGF- and Related Cytokines in Inflammation
~EN PB NW
ISBN: 9783034883542 bzw. 3034883544, vermutlich in Englisch, Taschenbuch, neu.
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