Isbn: 9781441918871 - multichain immune recognition receptor signaling: from spatiotemporal organization to human disease: 640 (10 risultati)

Taschenbuch. Condizione: Neu. Multichain Immune Recognition Receptor Signaling | From Spatiotemporal Organization to Human Disease | Alexander Sigalov | Taschenbuch | xxvii | Englisch | 2010 | Springer | EAN 9781441918871 | Verantwortliche Person für die EU: Springer Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg, juergen[dot]hartmann[at]springer[dot]com | Anbieter: preigu. …

Condizione: New. pp. 388.

Condizione: New. In English.

Taschenbuch. Condizione: Neu. Druck auf Anfrage Neuware - Printed after ordering - Immunological recognition is a central feature of the adaptive immunity of vertebrates. With the exception of agnathans, which developed an entirely distinct set of immunologically-specific molecules, all vertebrates use a recognition system based on what Achsah Keegan and I suggested in 1992 be termed multichain immune recognition receptors (MIRRs). MIRRs consist of ligand-binding molecules that are immunoglobulin supergene family members associated with signal transducers and enhancers in such a way as both insure precise ligand recognition, discrimination and ampHfication of the signal. Two of the prototypic sets of MIRRs, the T-cell and B-cell receptors, are among the most remarkable recognition molecules known. These are extraordinarily diverse molecules in which the range of ligands that can be potentially recognized prob ably exceeds the actual numbers of lymphocytes in the body. The discovery of the genetic basis of assembling these receptors and understanding how they bind to their cognate antigens are among the most stunning of scientific achievements. Yet these immensely specific binding chains (the heavy/light chain pair for immunoglobulin and the a/p chain pair for most T cells), when expressed as membrane molecules, have no obvious mechanism of signaling. For example, the iH chain cytosolic do main consists of three amino acids (lysine-valine-lysine) and the L chain is not even embedded in the membrane. Furthermore, there is no known direct mechanism to propagate information from the binding domain of the B-cell or T-cell receptors to the membrane-proximal domains of the same chains.…

Condizione: new. Questo è un articolo print on demand.

Taschenbuch. Condizione: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -Immunological recognition is a central feature of the adaptive immunity of vertebrates. With the exception of agnathans, which developed an entirely distinct set of immunologically-specific molecules, all vertebrates use a recognition system based on what Achsah Keegan and I suggested in 1992 be termed multichain immune recognition receptors (MIRRs). MIRRs consist of ligand-binding molecules that are immunoglobulin supergene family members associated with signal transducers and enhancers in such a way as both insure precise ligand recognition, discrimination and ampHfication of the signal. Two of the prototypic sets of MIRRs, the T-cell and B-cell receptors, are among the most remarkable recognition molecules known. These are extraordinarily diverse molecules in which the range of ligands that can be potentially recognized prob ably exceeds the actual numbers of lymphocytes in the body. The discovery of the genetic basis of assembling these receptors and understanding how they bind to their cognate antigens are among the most stunning of scientific achievements. Yet these immensely specific binding chains (the heavy/light chain pair for immunoglobulin and the a/p chain pair for most T cells), when expressed as membrane molecules, have no obvious mechanism of signaling. For example, the iH chain cytosolic do main consists of three amino acids (lysine-valine-lysine) and the L chain is not even embedded in the membrane. Furthermore, there is no known direct mechanism to propagate information from the binding domain of the B-cell or T-cell receptors to the membrane-proximal domains of the same chains. 388 pp. Englisch. …

Condizione: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. ALEXANDER SIGALOV, PhD, is a Research Assistant Professor in the Department of Pathology at the University of Massachusetts Medical School in Worcester, Massachusetts, USA. His main research interests include protein intrinsic disorder and oligomericity .…

Taschenbuch. Condizione: Neu. This item is printed on demand - Print on Demand Titel. Neuware -Immunological recognition is a central feature of the adaptive immunity of vertebrates. With the exception of agnathans, which developed an entirely distinct set of immunologically-specific molecules, all vertebrates use a recognition system based on what Achsah Keegan and I suggested in 1992 be termed multichain immune recognition receptors (MIRRs). MIRRs consist of ligand-binding molecules that are immunoglobulin supergene family members associated with signal transducers and enhancers in such a way as both insure precise ligand recognition, discrimination and ampHfication of the signal. Two of the prototypic sets of MIRRs, the T-cell and B-cell receptors, are among the most remarkable recognition molecules known. These are extraordinarily diverse molecules in which the range of ligands that can be potentially recognized prob ably exceeds the actual numbers of lymphocytes in the body. The discovery of the genetic basis of assembling these receptors and understanding how they bind to their cognate antigens are among the most stunning of scientific achievements. Yet these immensely specific binding chains (the heavy/light chain pair for immunoglobulin and the a/p chain pair for most T cells), when expressed as membrane molecules, have no obvious mechanism of signaling. For example, the |iH chain cytosolic do main consists of three amino acids (lysine-valine-lysine) and the L chain is not even embedded in the membrane. Furthermore, there is no known direct mechanism to propagate information from the binding domain of the B-cell or T-cell receptors to the membrane-proximal domains of the same chains.Springer-Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg 388 pp. Englisch.…

Condizione: New. Print on Demand pp. 388 70 Illus. (3 Col.).

Condizione: New. PRINT ON DEMAND pp. 388.