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TGF- and Related Cytokines in Inflammation Progress in Inflammation Research
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9783034895316 - TGF- and Related Cytokines in Inflammation Progress in Inflammation Research
1

TGF- and Related Cytokines in Inflammation Progress in Inflammation Research (?)

ISBN: 9783034895316 (?) bzw. 3034895313, in Deutsch, Birkhäuser, Taschenbuch, neu

86,30 + Versand: 3,55 = 89,85(unverbindlich)
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.
9783034895316 - TGF-SS and Related Cytokines in Inflammation (Paperback)
2

TGF-SS and Related Cytokines in Inflammation (Paperback) (2012) (?)

ISBN: 9783034895316 (?) bzw. 3034895313, in Deutsch, Springer Basel, Switzerland, Taschenbuch, neu, Nachdruck

94,09 + Versand: 1,36 = 95,45(unverbindlich)
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.
9783034895316 - Samuel N. Breit: TGF-SS and Related Cytokines in Inflammation
3
Samuel N. Breit (?):

TGF-SS and Related Cytokines in Inflammation (?)

ISBN: 9783034895316 (?) bzw. 3034895313, in Deutsch, Springer Basel, neu

82,94 (£ 71,99)¹(versandkostenfrei, unverbindlich)
in-stock
Von Händler/Antiquariat
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.
9783034895316 - Herausgegeben von Breit, Samuel N. Wahl, Sharon M.: TGF-ß and Related Cytokines in Inflammation
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Herausgegeben von Breit, Samuel N. Wahl, Sharon M. (?):

TGF-ß and Related Cytokines in Inflammation (?)

ISBN: 9783034895316 (?) bzw. 3034895313, in Deutsch, Birkhäuser, Taschenbuch, neu

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
9783034895316 - Samuel N. Breit; Sharon M. Wahl: TGF-β and Related Cytokines in Inflammation
5
Samuel N. Breit; Sharon M. Wahl (?):

TGF-β and Related Cytokines in Inflammation (?)

ISBN: 9783034895316 (?) bzw. 3034895313, in Deutsch, Springer Science+Business Media, neu

Lagernd
Von Händler/Antiquariat
biological, biology, cytokine, cytokines, growth, growth factor, inflammation, macrophages, molecule, protein, proteins, structure, Medicine & Public Health; Pathology, Book