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008    201008s2020    enk     o     000 0 eng d 
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020    9781839160691|q(PDF ebook) 
020    1839160691|q(PDF ebook) 
020    1839160772|q(ebook) 
020    9781839160776|q(electronic book) 
020    |z9781788016865|q(hardback) 
020    |z1788016866|q(hardback) 
035    (OCoLC)1199300020 
037    3-178-9781839160776|bIngram Content Group 
040    UIU|beng|erda|epn|cUIU|dUKRSC|dN$T|dEBLCP|dOCLCF|dUKMGB
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049    RIDW 
050  4 RS420 
082 04 615.19|223 
090    RS420 
245 00 Protein degradation with new chemical modalities :
       |bsuccessful strategies in drug discovery and chemical 
       biology /|cedited by Hilmar Weinmann, Craig Crews. 
264  1 Cambridge :|bRoyal Society of Chemistry,|c2020. 
300    1 online resource. 
336    text|btxt|2rdacontent 
337    computer|bc|2rdamedia 
338    online resource|bcr|2rdacarrier 
347    text file|2rdaft 
490 1  RSC drug discovery ;|v74 
505 0  Cover -- Half Title -- Series Information -- Title Page --
       Copyright Page -- Preface -- Contents -- Chapter 1 PROTAC-
       mediated Target Degradation: A Paradigm Changer in Drug 
       Discovery? -- References -- Chapter 2 Structural and 
       Biophysical Principles of Degrader Ternary Complexes -- 
       2.1 Introduction -- 2.1.1 Mechanistic Advantages of 
       Targeted Protein Degradation -- 2.1.1.1 Immediate 
       Advantages of Degradation Versus Inhibition -- 2.1.1.2 
       Differentiation of Degraders due to Their Mode of Action -
       - 2.1.2 History of PROTACs (2001-2010) -- 2.1.3 Small-
       molecule VHL- and CRBN-based PROTACs (2010-2015) 
505 8  2.2 Structural Features of Ternary Complexes -- 2.2.1 
       Ternary Complex Equilibria and Definitions -- 2.2.2 
       Structural Elucidation of PROTAC Ternary Complexes -- 
       2.2.2.1 The First PROTAC Ternary Complex Crystal Structure
       : VHL:MZ1:Brd4BD2 -- 2.2.2.2 Structure-guided design of 
       SMARCA2/4 PROTACs -- 2.2.2.3 Ternary Structures of CRBN-
       based PROTACs -- 2.2.3 Degraders as Monovalent Molecular 
       Glues -- 2.2.3.1 Cereblon-targeting Immunomodulatory Drugs
       -- 2.2.3.2 DCAF15-targeting Sulfonamide Drugs -- 2.2.4 
       Surface Areas Buried by PROTACs and Monovalent Glues -- 
       2.3 Ternary Assays 
505 8  2.3.1 Can My PROTAC Form a Ternary Complex? -- 2.3.1.1 
       Pull-down Assays -- 2.3.1.2 Proximity-based Ternary Assays
       : AlphaScreen/LISA and TR-FRET -- 2.3.1.3 Surface Plasmon 
       Resonance -- 2.3.2 How Tightly Does My Ternary Complex 
       Bind? -- 2.3.2.1 Competition Assays -- 2.3.2.2 Direct 
       Binding Assays -- 2.3.3 To What Extent Is My Ternary 
       Complex Cooperative? -- 2.3.4 How Long Does My Ternary 
       Complex Last? -- 2.3.5 Does the PROTAC Induce Ternary 
       Complex Formation in Cells? -- 2.3.5.1 Separation of 
       Phases-based Protein Interaction Reporter Assay (SPPIER) 
505 8  2.3.5.2 Bioluminescence Resonance Energy Transfer (BRET) -
       - 2.4 Concluding Remarks -- 2.5 Acknowledgments -- 2.5.1 
       Funding -- 2.5.2 Conflict of Interest Statement -- 
       References -- Chapter 3 Immediate and Selective Control of
       Protein Abundance Using the dTAG System -- 3.1 The 
       Potential and Limitations of Targeted Protein Degradation 
       -- 3.2 Chemical-Genetic Degradation Approaches -- 3.3 
       Development of the dTAG Platform -- 3.4 Genetic Methods to
       Express FKBP12F36V-fusions -- 3.4.1 Ectopic Expression of 
       FKBP12F36V-fusions -- 3.4.2 Knock-in Strategies to Express
       FKBP12F36V-fusions 
505 8  3.5 Strategies Towards Identification of a Lead dTAG 
       Molecule -- 3.5.1 Biochemical Assays for FKBP12F36V and E3
       Ligase Binding -- 3.5.2 Determining FKBP12F36V-specific 
       Degradation in Cells -- 3.5.3 Requirement of E3 Ligase and
       Proteasome -- 3.5.4 Assessment of dTAG Molecule 
       Selectivity -- 3.5.5 In Vivo Assessment of dTAG Molecule 
       Activity -- 3.6 Case Studies Employing the dTAG Platform -
       - 3.6.1 Target Validation Using dTAG -- 3.6.2 Targeting 
       Recalcitrant Oncoproteins Using dTAG -- 3.6.3 Targeting 
       Essential Transcriptional Regulators Using dTAG 
520    This book provides a comprehensive overview from the 
       leading academic and industrial experts on recent 
       developments, scope and limitations in this dynamically 
       growing research area; an ideal reference work for 
       researchers in drug discovery and chemical biology as well
       as advanced students. 
588 0  Print version record. 
590    eBooks on EBSCOhost|bEBSCO eBook Subscription Academic 
       Collection - North America 
650  0 Drugs|xDesign.|0https://id.loc.gov/authorities/subjects/
       sh88001157 
650  0 Proteolysis.|0https://id.loc.gov/authorities/subjects/
       sh2015000809 
650  7 Drugs|xDesign.|2fast|0https://id.worldcat.org/fast/898790 
650  7 Proteolysis.|2fast|0https://id.worldcat.org/fast/1930489 
650  7 Medication.|2homoit|0https://homosaurus.org/v3/
       homoit0001007 
655  0 Electronic books. 
655  4 Electronic books. 
700 1  Weinmann, Hilmar,|0https://id.loc.gov/authorities/names/
       n2003007544|eeditor. 
700 1  Crews, Craig,|0https://id.loc.gov/authorities/names/
       no2021095854|eeditor. 
776 08 |iPrint version:|tProtein degradation with new chemical 
       modalities|z9781788016865|w(OCoLC)1197735924 
830  0 RSC drug discovery series ;|0https://id.loc.gov/
       authorities/names/no2010092643|v74. 
856 40 |uhttps://rider.idm.oclc.org/login?url=https://
       search.ebscohost.com/login.aspx?direct=true&scope=site&
       db=nlebk&AN=2654401|zOnline ebook via EBSCO. Access 
       restricted to current Rider University students, faculty, 
       and staff. 
856 42 |3Instructions for reading/downloading the EBSCO version 
       of this ebook|uhttp://guides.rider.edu/ebooks/ebsco 
901    MARCIVE 20231220 
948    |d20220127|cEBSCO|tEBSCOebooksacademic NEW 6019|lridw 
994    92|bRID