LEADER 01385nam 2200349 n 450 001 996393251903316 005 20200824121656.0 035 $a(CKB)4940000000113443 035 $a(EEBO)2240889071 035 $a(UnM)ocm99886256e 035 $a(UnM)99886256 035 $a(EXLCZ)994940000000113443 100 $a19971112d1642 uh 101 0 $aeng 135 $aurbn||||a|bb| 200 10$aAt Edinburgh the first day of February, 1642$b[electronic resource] $eForsamekle [sic] as by the crueltie of the rebels in Ireland, great numbers of His Majesties good subjects, and our own countreymen there, are daily forced to flee out of Ireland to those parts in the west countrey, .. 210 $a[Edinburgh $cs.n.$d1642] 215 $a1 sheet ([1] p.) 300 $aImprint from Steele. 300 $aSteele notation: Maje- mie, manua-. 300 $aSigned at end: Arch Primerose, Cler., S.Cons. 300 $aReproduction of original in the British Library. 330 $aeebo-0018 607 $aScotland$xPolitics and government$y1625-1649$vEarly works to 1800 701 $aPrimrose$b Archibald$cSir,$f1616-1679.$01002093 712 02$aScotland.$bSovereign (1625-1649 : Charles I) 801 0$bCu-Riv 801 1$bCu-RivES 906 $aBOOK 912 $a996393251903316 996 $aAt Edinburgh the first day of February, 1642$92411274 997 $aUNISA LEADER 01199nam 2200325 450 001 996280525603316 005 20231208095044.0 010 $a0-7381-2353-6 035 $a(CKB)3780000000092691 035 $a(NjHacI)993780000000092691 035 $a(EXLCZ)993780000000092691 100 $a20231208d1993 uy 0 101 0 $aeng 135 $aur||||||||||| 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aIEEE standard for information technology $etest methods for measuring conformance to open systems interconnection (OSI) abstract data manipulation C language interfaces : binding for application program interface (API) /$fInstitute of Electrical and Electronics Engineers 210 1$aPiscataway, NJ :$cIEEE,$d1993. 215 $a1 online resource 517 $aIEEE Std 1224-1993: OSI Abstract Data Manipulation-API 606 $aC (Computer program language)$xStandards 615 0$aC (Computer program language)$xStandards. 676 $a005.133 801 0$bNjHacI 801 1$bNjHacl 906 $aDOCUMENT 912 $a996280525603316 996 $aIEEE standard for information technology$92574732 997 $aUNISA LEADER 05191nam 22006615 450 001 9910298353303321 005 20200703204609.0 010 $a1-4939-1130-9 024 7 $a10.1007/978-1-4939-1130-1 035 $a(CKB)3710000000228322 035 $a(EBL)1968583 035 $a(OCoLC)891386943 035 $a(SSID)ssj0001353649 035 $a(PQKBManifestationID)11750974 035 $a(PQKBTitleCode)TC0001353649 035 $a(PQKBWorkID)11316339 035 $a(PQKB)11392506 035 $a(MiAaPQ)EBC1968583 035 $a(DE-He213)978-1-4939-1130-1 035 $a(PPN)181351285 035 $a(EXLCZ)993710000000228322 100 $a20140901d2014 u| 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 14$aThe Molecular Chaperones Interaction Networks in Protein Folding and Degradation /$fedited by Walid A. Houry 205 $a1st ed. 2014. 210 1$aNew York, NY :$cSpringer New York :$cImprint: Springer,$d2014. 215 $a1 online resource (481 p.) 225 1 $aInteractomics and Systems Biology ;$v1 300 $aDescription based upon print version of record. 311 $a1-4939-1129-5 320 $aIncludes bibliographical references at the end of each chapters and index. 327 $aPart I: Global View of the Chaperone Network -- Analysis of Chaperone Network Throughput -- Part II: Chaperones at the Ribosome -- Functions of Ribosome-associated Chaperones and Their Interaction Network -- Part III: The Hsp 70 and Hsp40 Chaperone Networks -- Yeast Hsp70 and J-protein Chaperones: Function and Interaction Network -- The Chaperone Networks: An Hsp70 Perspective -- Part IV: The Hsp90 Chaperone Network -- The Interaction Network of the Hsp90 Molecular Chaperone -- A Global View of the Proteome Perturbations by Hsp90 Inhibitors -- Designing Drugs Against Hsp90 for Cancer Therapy -- The Candida albicans Hsp90 Chaperone Network is Environmentally Flexible and Evolutionarily Divergent -- Part V: The p23 Chaperone Network -- Emergence and Characterization of the p23 Molecular Chaperone -- Part VI: Chaperones in the ER: Function and Interaction Network -- Chaperones of the ERAD Pathway -- Chaperones and Proteases of Mitochondria: From Protein Folding and Degradation to Mitophagy -- Part VII: The Ubiquitin-Proteasome System Network -- The Biogenesis of the Eukaryotic Proteasome -- Systems-wide Analysis of Protein Ubiquitylation: We Finally Have the Tiger by the Tail -- Part VIII: The Chaperone and Protease Networks in Model Bacteria and Parasites -- The Interaction Networks of E. coli Chaperones -- Chaperone-Proteases of Mycobacteria -- The Interaction Networks of Hsp70 and Hsp90 in the Plasmodium and Leishmania Parasites -- Index. . 330 $aMolecular chaperones are a fundamental group of proteins that have been identified only relatively recently. They are key components of a protein quality machinery in the cell which insures that the folding process of any newly-synthesized polypeptide chain results in the formation of a properly folded protein and that the folded protein is maintained in an active conformation throughout its functional lifetime. Molecular chaperones have been shown to play essential roles in cell viability under both normal and stress conditions. Chaperones can also assist in the unfolding and degradation of misfolded proteins and in disaggregating preformed protein aggregates. Chaperones are also involved in other cellular functions including protein translocation across membranes, vesicle fusion events, and protein secretion. In recent years, tremendous advances have been made in our understanding of the biology, biochemistry, and biophysics of function of molecular chaperones. In addition, recent technical developments in the fields of proteomics and genomics allowed us to obtain a global view of chaperone interaction networks. Finally, there is now a growing interest in the role of molecular chaperones in diseases. This book will provide a comprehensive analysis of the structure and function of the diverse systems of molecular chaperones and their role in cell stress responses and in diseases from a global network perspective. . 410 0$aInteractomics and Systems Biology ;$v1 606 $aSystems biology 606 $aProteins 606 $aMedicine 606 $aSystems Biology$3https://scigraph.springernature.com/ontologies/product-market-codes/L15010 606 $aProtein Science$3https://scigraph.springernature.com/ontologies/product-market-codes/L14040 606 $aBiomedicine, general$3https://scigraph.springernature.com/ontologies/product-market-codes/B0000X 615 0$aSystems biology. 615 0$aProteins. 615 0$aMedicine. 615 14$aSystems Biology. 615 24$aProtein Science. 615 24$aBiomedicine, general. 676 $a570 676 $a572.6 676 $a610 702 $aHoury$b Walid A$4edt$4http://id.loc.gov/vocabulary/relators/edt 906 $aBOOK 912 $a9910298353303321 996 $aThe Molecular Chaperones Interaction Networks in Protein Folding and Degradation$92511881 997 $aUNINA