LEADER 01531nam a2200361 i 4500 001 991001130009707536 008 040402s ne 000 0 eng d 020 $a0444865217 035 $ab12722686-39ule_inst 040 $aDip.to Fisica$beng 082 0 $a539.7214 084 $aLC QC793.5.P622 084 $a53.3.5 110 2 $aInternational School of Physics "Enrico Fermi"$bMeeting$d<1981 ;$cVarenna, Italy>$0483620 245 10$aPositron solid-state physics :$bVarenna on Lake Como, Villa Monastero, 14-24 July 1981 /$cedited by W. Brandt 246 31$aPositoni nella fisica dei solidi 260 $aAmsterdam ;$aNew York :$bNorth-Holland Pub. Co.,$c1983 300 $axx, 710 p. :$bill. ;$c25 cm 440 $aProceedings of the International School of Physics "Enrico Fermi" ;$vcourse 83 440 $aRendiconti della Scuola Internazionale di Fisica "Enrico Fermi" ;$v83 500 $aAt head of title : Italian Physical Society 504 $aIncludes bibliographical references 650 4$aPositrons$xCongresses 650 4$aSolid state physics$xCongresses 650 4$aMetals$xSurfaces$xCongresses 700 1 $aBrandt, Werner 710 2 $aSocietą Italiana di Fisica 907 $a.b12722686$b07-07-16$c02-04-04 912 $a991001130009707536 945 $aLE006 53(042+082.2) VAR$g1$i2006000093170$lle006$o-$pE77.47$q-$rl$s- $t0$u0$v0$w0$x0$y.i13249915$z02-04-04 996 $aPositron solid-state physics$9267801 997 $aUNISALENTO 998 $ale006$b02-04-04$cm$da $e-$feng$gne $h0$i1 LEADER 04692nam 22006135 450 001 9910298340303321 005 20251117071627.0 010 $a1-4614-8317-4 024 7 $a10.1007/978-1-4614-8317-5 035 $a(CKB)3710000000074021 035 $a(EBL)1592886 035 $a(SSID)ssj0001086488 035 $a(PQKBManifestationID)11653535 035 $a(PQKBTitleCode)TC0001086488 035 $a(PQKBWorkID)11056070 035 $a(PQKB)10766546 035 $a(MiAaPQ)EBC1592886 035 $a(DE-He213)978-1-4614-8317-5 035 $a(PPN)176098607 035 $a(EXLCZ)993710000000074021 100 $a20131203d2014 u| 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 10$aProtein Deimination in Human Health and Disease /$fedited by Anthony P. Nicholas, Sanjoy K. Bhattacharya 205 $a1st ed. 2014. 210 1$aNew York, NY :$cSpringer New York :$cImprint: Springer,$d2014. 215 $a1 online resource (438 p.) 300 $aDescription based upon print version of record. 311 08$a1-4614-8316-6 320 $aIncludes bibliographical references and index. 327 $aPhysiological pathways of PAD activity and citrullinated epitope generation -- from citrullination to specific immunity and disease in rheumatoid arthritis -- The role of citrullinated proteins in the pathophysiology of rheumatoid arthritis -- Protein citrullination: the link between rheumatoid arthritis and periodontitis? -- From genes and environment to anti-culture immunity in rheumatoid arthritis: The role of the lungs -- Neutrophils and their contribution to autoimmunity in rheumatoid arthritis -- Deimination in skin and regulation of PAD expression in keratinocytes -- Importance of citrullination on hair protein molecular assembly during trichocytic differentiation -- Deimination in the peripheral nervous system: A wallflower existence -- Deimination in multiple sclerosis and experimental autoimmune encephalomyelitis -- Protein hypercitrullination in CNS demyelinating disease reversed by PAD inhibition -- Deimination in prion diseases -- Deimination in Alzheimer's disease -- Ongoing studies of deimination in neurodegenerative diseases using the F95 antibody -- The role of protein deimination in epigenetics -- Identifying citrullination sites by mass spectroscopy -- Homocitrulline?an analogue and confounder related to citrulline -- Picking the PAD lock: Chemical and biological approaches to identify PAD substrates and inhibitors. 330 $aDeimination is a relatively new post-translational modification of proteins, whose recognition is ever-increasing. First linked to the pathology of rheumatoid arthritis (RA), deimination is a process by which selected positively charged arginine amino acids are converted to neutral citrulline amino acids by the peptidyl arginine deiminase (PAD) family of enzymes. Although the medical literature is rich with articles about the possible significance of deiminated proteins in RA, Protein Deimination in Human Health and Disease is the first publication to compile this knowledge and the growing amount of new information now known about the presence of deiminated proteins in the eye, skin, hair, gums, lung and nervous system, as well. As a result, this process has now been linked to numerous additional conditions besides RA, including cancer, glaucoma, Alzheimer's disease, Parkinson's disease, multiple sclerosis, spinal cord and peripheral nerve injury, Creutzfeldt-Jakob disease, among many others. Chronicling the earliest studies of deimination up to the present, this volume distills what is currently known about citrullination of proteins in the human body and is the first book of its kind on the topic.  . 606 $aNeurosciences 606 $aImmunology 606 $aProteins 606 $aNeurosciences$3https://scigraph.springernature.com/ontologies/product-market-codes/B18006 606 $aImmunology$3https://scigraph.springernature.com/ontologies/product-market-codes/B14000 606 $aProtein Science$3https://scigraph.springernature.com/ontologies/product-market-codes/L14040 615 0$aNeurosciences. 615 0$aImmunology. 615 0$aProteins. 615 14$aNeurosciences. 615 24$aImmunology. 615 24$aProtein Science. 676 $a572.744 702 $aNicholas$b Anthony P.$4edt$4http://id.loc.gov/vocabulary/relators/edt 702 $aBhattacharya$b Sanjoy K$4edt$4http://id.loc.gov/vocabulary/relators/edt 906 $aBOOK 912 $a9910298340303321 996 $aProtein Deimination in Human Health and Disease$91954762 997 $aUNINA