HSF1 and Molecular Chaperones in Biology and Cancer

By:

Mendillo, Marc Laurence [Author]

Contributor(s):

Material type: Text

9783030402037

Subject(s):

Molecular chaperones

DDC classification:

572.633 23

Summary: Intro -- Preface: Dedication to Susan Lindquist -- Contents -- Part I: Structure -- 1: Structural and Biochemical Properties of Hsp40/Hsp70 Chaperone System -- 1.1 Hsp70 Chaperone System -- 1.1.1 Hsp70 Domain Structure and Functional Cycle -- 1.1.2 Substrate Recognition and Remodeling by the Hsp70 Chaperones -- 1.2 Regulation of Hsp70 Function by Co-chaperones -- 1.2.1 J-Domain Proteins -- 1.2.2 Nucleotide Exchange Factors -- 1.2.2.1 Nucleotide Cycle Regulation Beyond JDPs and NEFs -- 1.3 Hsp70s Interaction with Other Cellular Chaperone Systems -- 1.3.1 Hsp70 Chaperones in Protein Disaggregation -- 1.4 Conclusion and Perspectives -- References -- 2: The TRiC/CCT Chaperonin and Its Role in Uncontrolled Proliferation -- 2.1 Introduction -- 2.2 The Structure of CCT -- 2.3 CCT Substrates and Specificity -- 2.4 Conformational Changes and Nucleotide Hydrolysis -- 2.5 CCT and Cancer -- 2.6 CCT as Key Regulator of Cell Cycle -- 2.7 Is CCT a Possible Antiproliferation Target? -- References -- 3: Regulation of Hsf1 and the Heat Shock Response -- 3.1 Introduction: The HSR in Health and Disease -- 3.2 Defining the Transcriptional Response to Heat Shock -- 3.3 What Activates the HSR? -- 3.4 Hsp70 and Hsf1 Constitute a Negative Feedback Loop That Controls the HSR -- 3.5 Hsp90 Negatively Regulates Hsf1 Orthogonally to Hsp70 -- 3.6 Phosphorylation Is Dispensable for Hsf1 Activity During Heat Shock -- 3.7 Coordination of the HSR Across Tissues -- 3.8 Conclusion -- References -- Part II: Function -- 4: Challenging Proteostasis: Role of the Chaperone Network to Control Aggregation-Prone Proteins in Human Disease -- 4.1 Introduction -- 4.2 Molecular Chaperones and Protein Aggregation in Neurodegenerative Diseases -- 4.2.1 Amyloid-β -- 4.2.2 Tau -- 4.2.3 α-Synuclein -- 4.2.4 Polyglutamine Expansions -- 4.2.5 SOD1.

Holdings ( 1 )
Title notes ( 1 )

Holdings
Item type	Current library	Call number	Status	Date due	Barcode	Item holds
Book	Library	572-2020 (Browse shelf(Opens below))	Checked out	26/11/2025	AT-ISTA#003123

Total holds: 0

Intro -- Preface: Dedication to Susan Lindquist -- Contents -- Part I: Structure -- 1: Structural and Biochemical Properties of Hsp40/Hsp70 Chaperone System -- 1.1 Hsp70 Chaperone System -- 1.1.1 Hsp70 Domain Structure and Functional Cycle -- 1.1.2 Substrate Recognition and Remodeling by the Hsp70 Chaperones -- 1.2 Regulation of Hsp70 Function by Co-chaperones -- 1.2.1 J-Domain Proteins -- 1.2.2 Nucleotide Exchange Factors -- 1.2.2.1 Nucleotide Cycle Regulation Beyond JDPs and NEFs -- 1.3 Hsp70s Interaction with Other Cellular Chaperone Systems -- 1.3.1 Hsp70 Chaperones in Protein Disaggregation -- 1.4 Conclusion and Perspectives -- References -- 2: The TRiC/CCT Chaperonin and Its Role in Uncontrolled Proliferation -- 2.1 Introduction -- 2.2 The Structure of CCT -- 2.3 CCT Substrates and Specificity -- 2.4 Conformational Changes and Nucleotide Hydrolysis -- 2.5 CCT and Cancer -- 2.6 CCT as Key Regulator of Cell Cycle -- 2.7 Is CCT a Possible Antiproliferation Target? -- References -- 3: Regulation of Hsf1 and the Heat Shock Response -- 3.1 Introduction: The HSR in Health and Disease -- 3.2 Defining the Transcriptional Response to Heat Shock -- 3.3 What Activates the HSR? -- 3.4 Hsp70 and Hsf1 Constitute a Negative Feedback Loop That Controls the HSR -- 3.5 Hsp90 Negatively Regulates Hsf1 Orthogonally to Hsp70 -- 3.6 Phosphorylation Is Dispensable for Hsf1 Activity During Heat Shock -- 3.7 Coordination of the HSR Across Tissues -- 3.8 Conclusion -- References -- Part II: Function -- 4: Challenging Proteostasis: Role of the Chaperone Network to Control Aggregation-Prone Proteins in Human Disease -- 4.1 Introduction -- 4.2 Molecular Chaperones and Protein Aggregation in Neurodegenerative Diseases -- 4.2.1 Amyloid-β -- 4.2.2 Tau -- 4.2.3 α-Synuclein -- 4.2.4 Polyglutamine Expansions -- 4.2.5 SOD1.