Bibliografías temáticas / Ligand Recognition / Libros

Libros sobre el tema "Ligand Recognition"

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Autor: Grafiati
Publicado: 6 de septiembre de 2023

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1

Neidle, Stephen. DNA structure and recognition. Oxford, Eng: IRL Press at Oxford University Press, 1994.

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2

Hans-Joachim, Böhm y Schneider Gisbert 1965-, eds. Protein-ligand interactions from molecular recognition to drug design. Weinheim: Wiley-VCH, 2003.

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3

Nicolae, Voiculetz, Motoc Ioan 1950- y Simon Zeno, eds. Specific interactions and biological recognition processes. Boca Raton: CRC Press, 1993.

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4

Makarem, Rima. Regulation and molecular basis of ligand recognition by the integrin [alpha]4[beta]1. Manchester: University of Manchester, 1993.

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5

William, Hutchens T., J.T. Baker Chemical Co. y University of California, Los Angeles., eds. Protein recognition of immobilized ligands: Proceedings of a J.T. Baker-UCLA Colloquium, held at Santa Fe, New Mexico, December 2-7, 1987. New York: A.R. Liss, 1989.

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6

Schneider, Gisbert, Gerd Folkers, Raimund Mannhold, Hugo Kubinyi y Hans-Joachim B�hm. Protein-Ligand Interactions: From Molecular Recognition to Drug Design. Wiley & Sons, Limited, John, 2005.

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7

Schneider, Gisbert, Gerd Folkers, Raimund Mannhold, Hugo Kubinyi y Hans-Joachim B�hm. Protein-Ligand Interactions: From Molecular Recognition to Drug Design. Wiley & Sons, Incorporated, John, 2006.

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8

Nucleic Acid Structure and Recognition. Oxford University Press, USA, 2002.

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9

Su, Ruey-Chyi. Major histocompatibility complex class I as a ligand for natural killer cell recognition. 2000.

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10

DNA Structure and Recognition (IN FOCUS). Oxford University Press, USA, 1994.

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11

Schafer, Jamie Lynn. Rhesus macaque KIR recognition of MHC class I molecules: Ligand identification and modulation of interaction by SIV peptides. 2014.

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12

Knaggs, Roger D. The molecular structure of the μ‎-opioid receptor. Editado por Paul Farquhar-Smith, Pierre Beaulieu y Sian Jagger. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780198834359.003.0038.

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The landmark paper discussed in this chapter describes the crystal structure of the μ‎-opioid receptor (also known as MOP-1). Opioids are some of the oldest known drugs and have been used for over 4,000 years; however, in addition to having beneficial analgesic effects, they are associated with a myriad of side effects that can minimize their use. Although the gene sequences of the opioid receptors were determined in the 1990s it has taken much longer to translate this into visualizing their three-dimensional structure. The μ‎-opioid receptor consists of seven transmembrane α‎-helices that are connected by three extracellular loops and three intracellular loops, with a wide open binding pocket which offers many potential ligand interaction sites, and evidence of dimerization. Understanding the crystal structure of the μ‎-opioid receptor in much more detail aids explanation of the molecular determinants of ligand recognition and selectivity and will be of use in designing novel opioids with improved efficacy and fewer side effects.
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13

Hutchens, William. Protien Recognition of Immobolized Ligands. John Wiley & Sons Inc, 2000.

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14

Ang, Xiaolu Lulu Lim. Substrates of the SCF-beta-TRCP E3 ubiquitin ligase complex: Mechanisms of recognition and delivery to the proteasome. 2009.

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15

Studnicki, Lisa H. Stereospecific epoxidation and epoxide hydrolysis: I.C2-symmetric ligands for mononuclear Ti(IV) complexes. II. Stereospecific recognition of aziridines: implication on epoxide hydrolysis. 2002.

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16

Colbert, Robert A. y Paul Bowness. Immune mechanisms: HLA-B27. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780198734444.003.0006.

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HLA-B27 is present in the majority of patients with ankylosing spondylitis (AS). Although we have learned a considerable amount about the natural immunologic function of HLA class I proteins, this has not provided a definitive mechanism of AS pathogenesis. While HLA-B27 is adept at presenting antigenic peptides to CD8+ T cells, ‘arthritogenic’ peptides targeted by a cross-reactive T or natural killer cell response have not been described, nor have autoreactive T cells been found. Newer concepts have evolved based on the propensity of HLA-B27 to ‘misbehave’, both inside cells and on the cell surface. Misfolded HLA-B27 molecules may stimulate an endoplasmic reticulum stress response, promoting production of IL-23 and then IL-17 and related cytokines. Aberrant cell-surface HLA-B27 molecules are ligands for natural killer and related immunoreceptors, and recognition can lead to IL-17 proinflammatory responses. There is growing evidence to suggest that these aberrant behaviours contribute to AS pathogenesis.
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