Isbn: 9780387097886 - multichain immune recognition receptor signaling: from spatiotemporal organization to human disease: 640 (11 risultati)

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  • Lingua: Inglese

    Editore: Springer, 2008

    0387097880 / 9780387097886

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  • Lingua: Inglese

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    Condizione: Used. pp. xxxvii + 169 1st Edition.

  • Lingua: Inglese

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    Condizione: Used. pp. xxxvii + 169 Illus.

  • Lingua: Inglese

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    Condizione: Used. pp. xxxvii + 169.

  • Lingua: Inglese

    Editore: Springer New York, 2008

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    Condizione: Sehr gut. Zustand: Sehr gut | Seiten: 388 | Sprache: Englisch | Produktart: Bücher | 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.

  • Lingua: Inglese

    Editore: Springer, 2008

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    Buch. 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.

  • Lingua: Inglese

    Editore: Springer, 2009

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    Hardcover. Condizione: Like New. LIKE NEW. SHIPS FROM MULTIPLE LOCATIONS. book.

  • Lingua: Inglese

    Editore: Springer New York Okt 2008, 2008

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    Da: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, GermaniaBuchWeltWeit Ludwig Meier e.K.

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    Buch. 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.

  • Lingua: Inglese

    Editore: Springer New York, 2008

    0387097880 / 9780387097886

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    Gebunden. 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 .

  • Lingua: Inglese

    Editore: Springer New York, Springer New York Okt 2008, 2008

    0387097880 / 9780387097886

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    Buch. 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.