MARC Record from Library of Congress

LEADER: 04400cam a2200469 a 4500
001 2010050245
003 DLC
005 20120327083216.0
008 101124s2011 nyua b 001 0 eng
010 $a 2010050245
016 7 $a101548333$2DNLM
016 7 $a015706500$2Uk
020 $a9781441984135 (hardback)
020 $a1441984135 (hardback)
035 $a(OCoLC)ocn688679726
040 $aDNLM/DLC$cDLC$erda$dYDX$dNLM$dYDXCP$dIXA$dUKMGB$dMMU$dDLC
050 00 $aQP609.C94$bC965 2011
060 10 $aW1$bAD559 v.712 2011
060 10 $aQU 136
082 00 $a616.9/041$222
245 00 $aCysteine proteases of pathogenic organisms /$cedited by Mark W. Robinson, PhD, Infection, Immunity and Innovation (i3) Institute, University of Technology Sydney, Ultimo, Sydney, Australia, John P. Dalton, PhD, Institute of Parasitology, McDonald Campus, McGill University, St. Anne de Bellevue, Quebec, Canada.
260 $aNew York :$bSpringer Science+Business Media ;$aAustin, Tex. :$bLandes Bioscience,$c©2011.
300 $axix, 226 pages :$billustrations ;$c27 cm.
336 $atext$2rdacontent
337 $aunmediated$2rdamedia
338 $avolume$2rdacarrier
490 1 $aAdvances in experimental medicine and biology ;$vv. 712
504 $aIncludes bibliographical references and index.
500 $aMachine generated contents note: Papa In Like Proteases Of Staphylococcus Aureus.- The Lysine Specific Gingipain Of Porphyromonas: Importance To Pathogenicity.- Falcipains And Other Cysteine Proteases Of Malaria Parasites.- Cathepsin Proteases In Toxoplasma Gondii.- Entamoeba Histolytica Cathepsin Like Enzymes.- Cysteine Peptidases Of Kinetoplastid Parasites.- Cruzain: The Path From Target Validation To The Clinic.- The Phylogeny, Structure And Function Of Trematode Cysteine Proteases, With Particular Emphasis On The Fasciola Hepatica Cathepsin L Family.- Cathepsins B1 And B2 Of Trichobilharzia Spp., Bird Schistosomes Causing Cercarial Dermatitis.- Proteases In Blood Feeding Nematodes And Their Potential As Vaccine Candidates.- Cysteine Proteases From Bloodfeeding Arthropod Ectoparasites.- How Pathogen Derived Cysteine Proteases Modulate Host Immune Responses.- Cystatins Of Parasitic Organisms.
520 $aCysteine proteases expressed by pathogenic organisms play key roles in virulence including host entry, feeding and suppression of host immune responses. This book gives comprehensive coverage to all aspects of pathogen cysteine proteases and brings together numerous scientific advances which have been made over many years. Thus, the biochemistry, molecular biology and structure function relationships of these important pathogen enzymes are covered in detail. Written by leading researchers from Europe, Australia and North America, this book is essential reading for students and professionals interested in human medicine and infectious disease research --Provided by publisher.
505 0 $aPapain-like proteases of staphylococcus aureus -- Lysine specific gingipain of Porphyromonas gingivalis: importance to pathogenicity and potential strategies for inhibition -- Falcipains and other cysteine proteases of malaria parasites -- Cathepsin proteases in Toxoplasma gondii -- Entamoeba Histolytica cathepsin-like enzymes -- Cysteine peptidases of kinetoplastid parasites -- Cruzain: the path from target validation to the clinic -- Phylogeny, structure and function of trematode cysteine proteases, with particular emphasis on the Fasciola hepatica cathepsin L family -- Cathepsins B1 and B2 of Trichobilharzia spp., bird schistosomes causing cercarial dermatitis -- Proteases in blood feeding nematodes and their potential as vaccine candidates -- Cysteine proteases from bloodfeeding arthropod ectoparasites -- How pathogen derived cysteine proteases modulate host immune responses -- Cystatins of parasitic organisms.
650 0 $aCysteine proteinases$xPathophysiology.
650 0 $aMicrobial enzymes.
650 0 $aPathogenic microorganisms.
650 12 $aCysteine Proteases$xchemistry.
650 22 $aBacteria$xenzymology.
650 22 $aCysteine Proteases$ximmunology.
650 22 $aEukaryota$xenzymology.
650 22 $aViruses$xenzymology.
700 1 $aRobinson, Mark W.$q(Mark William),$d1977-$eeditor.
700 1 $aDalton, J. P.$q(John Pius),$d1958-$eeditor.
830 0 $aAdvances in experimental medicine and biology ;$vv. 712.