LEADER 01938nam2 2200385 i 450 001 SUN0125360 005 20200305121941.243 010 $d0.00 017 70$2N$a978-3-319-10193-4 100 $a20191106d2015 |0engc50 ba 101 $aeng 102 $aCH 105 $a|||| ||||| 200 1 $a<> 1$fArnold Koslow, Arthur Buchsbaum editors 205 $aCham : Birkhäuser, 2015 210 $aXII$d520 p.$cill. ; 24 cm 215 $aPubblicazione in formato elettronico 410 1$1001SUN0103951$12001 $a*Studies in Universal Logic$1210 $aBasel$cBirkhäuser$d2008-. 461 1$1001SUN0113376$12001 $aThe *road to universal logic$efestschrift for the 50. birthday of Jean-Yves Béziau$fArnold Koslow, Arthur Buchsbaum$v1$1210 $aCham$cBirkhäuser$d2015$1215 $avoll.$cill.$d24 cm. 606 $a01Axx$xHistory of mathematics and mathematicians [MSC 2020]$2MF$3SUNC019751 606 $a03G30$xCategorical logic, topoi [MSC 2020]$2MF$3SUNC024384 606 $a03A05$xPhilosophical and critical aspects of logic and foundations [MSC 2020]$2MF$3SUNC024501 606 $a03B22$xAbstract deductive systems [MSC 2020]$2MF$3SUNC033624 606 $a03B42$xLogics of knowledge and belief (including belief change) [MSC 2020]$2MF$3SUNC033625 606 $a03B62$xCombined logics [MSC 2020]$2MF$3SUNC033626 620 $aCH$dCham$3SUNL001889 702 1$aKoslow$b, Arnold$3SUNV087513 702 1$aBuchsbaum$b, Arthur$3SUNV087514 712 $aBirkhäuser$3SUNV000319$4650 801 $aIT$bSOL$c20210503$gRICA 856 4 $uhttp://doi.org/10.1007/978-3-319-10193-4 912 $aSUN0125360 950 $aUFFICIO DI BIBLIOTECA DEL DIPARTIMENTO DI MATEMATICA E FISICA$d08CONS e-book 0481 $e08eMF481 20191107 996 $aRoad to universal logic$91564638 997 $aUNICAMPANIA LEADER 00943cam a2200253 i 4500 001 991002650979707536 008 030219s2004 it 000 0 ita d 020 $a8846452313 035 $ab12956260-39ule_inst 040 $aDip.to Studi Storici$bita 082 0 $a306.87 100 1 $aSolinas, Pier Giorgio$0103063 245 12$aL'acqua strangia :$bil declino della parentela nella società complessa /$cPier Giorgio Salinas 260 $aMilano :$bFranco Angeli,$cc2004 300 $a221 p. ;$c23 cm 440 0$aAntropologia culturale e sociale 650 4$aSociologia della famiglia 650 4$aParentela$xStudi antropologici 907 $a.b12956260$b02-04-14$c12-07-04 912 $a991002650979707536 945 $aLE023 306.87 SOL 1 1$g1$i2023000067628$lle023$o-$pE20.00$q-$rl$s- $t0$u1$v0$w1$x0$y.i13837321$z10-09-04 996 $aAcqua strangia$9279914 997 $aUNISALENTO 998 $ale023$b12-07-04$cm$da $e-$fita$git $h0$i0 LEADER 05467nam 22006734a 450 001 9911019958303321 005 20200520144314.0 010 $a9786610520947 010 $a9781280520945 010 $a1280520949 010 $a9783527606122 010 $a3527606122 010 $a9783527606283 010 $a3527606289 035 $a(CKB)1000000000375903 035 $a(EBL)481363 035 $a(SSID)ssj0000167130 035 $a(PQKBManifestationID)11171490 035 $a(PQKBTitleCode)TC0000167130 035 $a(PQKBWorkID)10169595 035 $a(PQKB)10273779 035 $a(MiAaPQ)EBC481363 035 $a(OCoLC)85820688 035 $a(Perlego)2761363 035 $a(EXLCZ)991000000000375903 100 $a20040909d2004 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aHandbook of ATPases $ebiochemistry, cell biology, pathophysiology /$fedited by Masamitsu Futai, Yoh Wada, and Jack H. Kaplan 210 $aWeinheim $cWiley-VCH$dc2004 215 $a1 online resource (495 p.) 300 $aDescription based upon print version of record. 311 08$a9783527306893 311 08$a3527306897 320 $aIncludes bibliographical references and index. 327 $aHandbook of ATPases; Contents; Preface; List of Contributors; Part I P-type ATPases; 1 Yeast Plasma-membrane H(+)-ATPase: Model System for Studies of Structure, Function, Biogenesis, and Regulation; 1.1 Introduction; 1.2 Structure; 1.2.1 Ca(2+)-ATPase as a Model; 1.2.2 Applicability of the Ca(2+)-ATPase Structure to Other P(2)-ATPases, Including the Pma1 H(+)-ATPase; 1.2.3 H(+)-ATPase Oligomers; 1.2.4 Associated Proteolipids; 1.3 Reaction Mechanism; 1.3.1 Overview of the Reaction Cycle; 1.3.2 ATP Binding and Phosphorylation; 1.3.3 E1-E2 Conformational Change; 1.3.4 H(+) Pumping 327 $a1.4 Biogenesis1.4.1 Pma1 Mutants with Defects in Folding and Biogenesis; 1.4.2 Use of Pma1 Mutants to Screen for Other Genes that Play a Role in Biogenesis and Quality Control; 1.4.3 Role of Lipid Rafts; 1.5 Regulation; 1.6 Emerging Knowledge of Other Yeast P-type ATPases; Acknowledgments; References; 2 Regulation of the Sarco(endo)plasmic Reticulum Ca(2+)-ATPase by Phospholamban and Sarcolipin; 2.1 Introduction; 2.1.1 Background to Ca(2+) Signaling; 2.1.2 ?-Adrenergic Signaling in the Heart; 2.2 Phospholamban-SERCA Interactions; 2.2.1 SERCA Structure and Function 327 $a2.2.2 PLN Structure and Function2.2.3 Approaches to the Study of PLN-SERCA Interactions; 2.2.4 SERCA Residues Essential for Cytoplasmic Interaction with PLN; 2.2.5 PLN Residues Essential for Cytoplasmic Interaction with SERCA; 2.2.6 PLN Residues Essential for Transmembrane Interactions with SERCA; 2.2.7 SERCA Residues Essential for Transmembrane Interactions with PLN; 2.2.8 Structural Modeling of the PLN-SERCA Inhibitory Interaction; 2.3 Physiological Role of PLN in Basal Cardiac Function; 2.3.1 Alterations in PLN Levels and Function by Transcription and Phosphorylation 327 $a2.3.2 Targeting of PLN2.3.3 Role of PLN in Smooth and Skeletal Muscles; 2.3.4 Overexpression of PLN; 2.3.5 Physiological Role of PLN in ?-Adrenergic Stimulation; 2.3.6 Superinhibitory PLN Mutants; 2.4 Phospholamban in Heart Failure; 2.4.1 Introduction; 2.4.2 Potential Therapies; 2.5 Human PLN Mutations as a Cause of Cardiomyopathy; 2.5.1 PLN R9C Mutant; 2.5.2 PLN L39stop Mutant; 2.6 Sarcolipin; 2.6.1 Introduction; 2.7 Physiological Role of SLN; 2.7.1 SLN Expression; 2.7.2 Overexpression of SLN; 2.7.2.1 Response of the SLN Gene to Chronic Stimulation 327 $a2.7.3 Inhibition of SERCA Function by SLN Plus PLN2.7.4 Modeling of the SLN-SERCA and SLN-PLN-SERCA Interactions; Acknowledgments; References; 3 Catalytic and Transport Mechanism of the Sarco-(Endo)Plasmic Reticulum Ca(2+)-ATPase (SERCA); Summary; 3.1 Introduction; 3.2 Experimental Systems; 3.3 Functional Characterization; 3.4 Structural Characterization; 3.4.1 Extramembranous Region and the Catalytic Domains of E1·2Ca(2+); 3.4.2 Transmembrane region of E1·2Ca(2+); 3.4.3 Enzyme Structure in the Absence of Ca(2+) (E2·TG); 3.4.4 Thapsigargin-binding Domain; 3.4.5 Interaction with Phospholamban 327 $a3.5 Binding of Ligands, Catalytic Events and Conformational Changes 330 $aAs the first comprehensive overview of this important class of enzymes, this two-volume handbook summarizes recent knowledge about the molecular mechanism of ATPases, relating this information to the physiology and pathopyhsiology of ion transport, mitochondrial function, vesicle transport and lysosomal acidification. All important P-type, F-type and V-type ATPases are treated systematically, complemented by a special section on the cell biology and physiology of acidic compartments, and backed by an extensive bibliography and index. This premier reference source for physiologists, molecular 606 $aAdenosine triphosphatase$vHandbooks, manuals, etc 606 $aAdenosine triphosphatase$xPathophysiology$vHandbooks, manuals, etc 615 0$aAdenosine triphosphatase 615 0$aAdenosine triphosphatase$xPathophysiology 676 $a572/.475 701 $aWada$b Yoh$01841957 701 $aKaplan$b Jack H$01841958 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9911019958303321 996 $aHandbook of ATPases$94421881 997 $aUNINA