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010   $a81-322-2467-1
024 7 $a10.1007/978-81-322-2467-9
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035   $a(PQKBTitleCode)TC0001583879
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035   $a(DE-He213)978-81-322-2467-9
035   $a(MiAaPQ)EBC4179017
035   $a(PPN)190516933
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100   $a20151126d2015      u|             0
101 0 $aeng
135   $aur|n|---|||||
181   $ctxt
182   $cc
183   $acr
200 10$aProteostasis and Chaperone Surveillance$b[electronic resource] /$fedited by Laishram Rajendrakumar Singh, Tanveer Ali Dar, Parvaiz Ahmad
205   $a1st ed. 2015.
210  1$aNew Delhi :$cSpringer India :$cImprint: Springer,$d2015.
215   $a1 online resource (184 p.)
300   $aDescription based upon print version of record.
311   $a81-322-2466-3 
320   $aIncludes bibliographical references at the end of each chapters.
327   $aPart 1: Maintaining Proteostasis -- 1. Structural Allostery and Protein-Protein Interactions of Sin3 -- 2. Protein Posttranslational Modifications: Role in Protein Structure, Function and Stability -- 3. Protein Folding and Aggregation: A revisit of basic conception -- Part 2: Proteopathy: Failure of proteostasis -- 4. Protein Folding: From Normal Cellular Function to Pathophysiology -- 5. Protein Misfolding Diseases: In perspective of Gain and loss-of-function -- 6. Amyloid formation in Alzheimer?s disease -- 7. Advances in modulation of Proteopathies, the devil spread from head to toe -- Part 3: Chaperone surveillance of proteopathy -- 8. Small Molecule Osmolytes can Modulate Proteostasis -- 9. Pharmacological Chaperones in Protein Aggregation Disorders.
330   $aProteostasis is central to the development of various human diseases caused due to excessive protein misfolding and the disregulation of the protein quality control system. In this book, respected researchers from many leading institutions contribute their insights on proteostasis maintenance. The coverage mainly focuses on the basics of maintaining proteostasis, the consequences of proteostatic system failure, and how chaperone systems constantly maintain proteostasis. In addition, the book presents in detail different treatment strategies for diseases caused by proteostatic system failure, as well as the inhibition of proteostatic failure using small molecule compounds. It examines advances in the modulation of proteopathies, providing a comprehensive source of key mechanistic insights on these diseases. As such, the book offers a valuable resource for beginners and more experienced investigators alike who are looking for detailed and reliable information on protein homeostasis, the diseases that can develop due to related imbalances, and the essential role of molecular and chemical chaperones.
606   $aProteins 
606   $aProteomics
606   $aProtein Science$3https://scigraph.springernature.com/ontologies/product-market-codes/L14040
606   $aProtein Structure$3https://scigraph.springernature.com/ontologies/product-market-codes/L14050
606   $aProteomics$3https://scigraph.springernature.com/ontologies/product-market-codes/L1403X
606   $aProtein-Ligand Interactions$3https://scigraph.springernature.com/ontologies/product-market-codes/L14060
615  0$aProteins .
615  0$aProteomics.
615 14$aProtein Science.
615 24$aProtein Structure.
615 24$aProteomics.
615 24$aProtein-Ligand Interactions.
676   $a570
702   $aSingh$b Laishram Rajendrakumar$4edt$4http://id.loc.gov/vocabulary/relators/edt
702   $aDar$b Tanveer Ali$4edt$4http://id.loc.gov/vocabulary/relators/edt
702   $aAhmad$b Parvaiz$4edt$4http://id.loc.gov/vocabulary/relators/edt
906   $aBOOK
912   $a9910298448403321
996   $aProteostasis and Chaperone Surveillance$92544122
997   $aUNINA