Protein degradation with new chemical modalities :: successful strategies in drug discovery and chemical biology /
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.
Gespeichert in:
| Weitere Verfasser: | , |
|---|---|
| Format: | Elektronisch E-Book |
| Sprache: | English |
| Veröffentlicht: |
Cambridge :
Royal Society of Chemistry,
2020.
|
| Schriftenreihe: | RSC drug discovery series ;
74. |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Zusammenfassung: | 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. |
| Beschreibung: | 1 online resource |
| ISBN: | 9781839160691 1839160691 1839160772 9781839160776 |
Internformat
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| 245 | 0 | 0 | |a Protein degradation with new chemical modalities : |b successful strategies in drug discovery and chemical biology / |c edited by Hilmar Weinmann, Craig Crews. |
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| 505 | 0 | |a 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 | |a 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 | |a 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 | |a 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 | |a 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 | |a 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. | ||
| 650 | 0 | |a Drugs |x Design. |0 http://id.loc.gov/authorities/subjects/sh88001157 | |
| 650 | 0 | |a Proteolysis. |0 http://id.loc.gov/authorities/subjects/sh2015000809 | |
| 650 | 2 | |a Drug Design |0 https://id.nlm.nih.gov/mesh/D015195 | |
| 650 | 2 | |a Proteolysis |0 https://id.nlm.nih.gov/mesh/D059748 | |
| 650 | 6 | |a Médicaments |x Conception. | |
| 650 | 6 | |a Protéolyse. | |
| 650 | 7 | |a Drugs |x Design |2 fast | |
| 650 | 7 | |a Proteolysis |2 fast | |
| 700 | 1 | |a Weinmann, Hilmar, |e editor. |0 http://id.loc.gov/authorities/names/n2003007544 | |
| 700 | 1 | |a Crews, Craig, |e editor. | |
| 758 | |i has work: |a Protein degradation with new chemical modalities (Text) |1 https://id.oclc.org/worldcat/entity/E39PCGHQB4XbPwR9FQBQ33qHhb |4 https://id.oclc.org/worldcat/ontology/hasWork | ||
| 776 | 0 | 8 | |i Print version: |t Protein degradation with new chemical modalities |z 9781788016865 |w (OCoLC)1197735924 |
| 830 | 0 | |a RSC drug discovery series ; |v 74. |0 http://id.loc.gov/authorities/names/no2010092643 | |
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Datensatz im Suchindex
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| contents | 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) 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 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) 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 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 |
| ctrlnum | (OCoLC)1199300020 |
| dewey-full | 615.19 |
| dewey-hundreds | 600 - Technology (Applied sciences) |
| dewey-ones | 615 - Pharmacology and therapeutics |
| dewey-raw | 615.19 |
| dewey-search | 615.19 |
| dewey-sort | 3615.19 |
| dewey-tens | 610 - Medicine and health |
| discipline | Medizin |
| format | Electronic eBook |
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| illustrated | Not Illustrated |
| indexdate | 2024-11-27T13:30:05Z |
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| isbn | 9781839160691 1839160691 1839160772 9781839160776 |
| language | English |
| oclc_num | 1199300020 |
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| series | RSC drug discovery series ; |
| series2 | RSC drug discovery ; |
| spelling | Protein degradation with new chemical modalities : successful strategies in drug discovery and chemical biology / edited by Hilmar Weinmann, Craig Crews. Cambridge : Royal Society of Chemistry, 2020. 1 online resource text txt rdacontent computer c rdamedia online resource cr rdacarrier RSC drug discovery ; 74 Print version record. 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) 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 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) 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 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 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. Drugs Design. http://id.loc.gov/authorities/subjects/sh88001157 Proteolysis. http://id.loc.gov/authorities/subjects/sh2015000809 Drug Design https://id.nlm.nih.gov/mesh/D015195 Proteolysis https://id.nlm.nih.gov/mesh/D059748 Médicaments Conception. Protéolyse. Drugs Design fast Proteolysis fast Weinmann, Hilmar, editor. http://id.loc.gov/authorities/names/n2003007544 Crews, Craig, editor. has work: Protein degradation with new chemical modalities (Text) https://id.oclc.org/worldcat/entity/E39PCGHQB4XbPwR9FQBQ33qHhb https://id.oclc.org/worldcat/ontology/hasWork Print version: Protein degradation with new chemical modalities 9781788016865 (OCoLC)1197735924 RSC drug discovery series ; 74. http://id.loc.gov/authorities/names/no2010092643 FWS01 ZDB-4-EBA FWS_PDA_EBA https://search.ebscohost.com/login.aspx?direct=true&scope=site&db=nlebk&AN=2654401 Volltext |
| spellingShingle | Protein degradation with new chemical modalities : successful strategies in drug discovery and chemical biology / RSC drug discovery series ; 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) 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 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) 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 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 Drugs Design. http://id.loc.gov/authorities/subjects/sh88001157 Proteolysis. http://id.loc.gov/authorities/subjects/sh2015000809 Drug Design https://id.nlm.nih.gov/mesh/D015195 Proteolysis https://id.nlm.nih.gov/mesh/D059748 Médicaments Conception. Protéolyse. Drugs Design fast Proteolysis fast |
| subject_GND | http://id.loc.gov/authorities/subjects/sh88001157 http://id.loc.gov/authorities/subjects/sh2015000809 https://id.nlm.nih.gov/mesh/D015195 https://id.nlm.nih.gov/mesh/D059748 |
| title | Protein degradation with new chemical modalities : successful strategies in drug discovery and chemical biology / |
| title_auth | Protein degradation with new chemical modalities : successful strategies in drug discovery and chemical biology / |
| title_exact_search | Protein degradation with new chemical modalities : successful strategies in drug discovery and chemical biology / |
| title_full | Protein degradation with new chemical modalities : successful strategies in drug discovery and chemical biology / edited by Hilmar Weinmann, Craig Crews. |
| title_fullStr | Protein degradation with new chemical modalities : successful strategies in drug discovery and chemical biology / edited by Hilmar Weinmann, Craig Crews. |
| title_full_unstemmed | Protein degradation with new chemical modalities : successful strategies in drug discovery and chemical biology / edited by Hilmar Weinmann, Craig Crews. |
| title_short | Protein degradation with new chemical modalities : |
| title_sort | protein degradation with new chemical modalities successful strategies in drug discovery and chemical biology |
| title_sub | successful strategies in drug discovery and chemical biology / |
| topic | Drugs Design. http://id.loc.gov/authorities/subjects/sh88001157 Proteolysis. http://id.loc.gov/authorities/subjects/sh2015000809 Drug Design https://id.nlm.nih.gov/mesh/D015195 Proteolysis https://id.nlm.nih.gov/mesh/D059748 Médicaments Conception. Protéolyse. Drugs Design fast Proteolysis fast |
| topic_facet | Drugs Design. Proteolysis. Drug Design Proteolysis Médicaments Conception. Protéolyse. Drugs Design |
| url | https://search.ebscohost.com/login.aspx?direct=true&scope=site&db=nlebk&AN=2654401 |
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