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E-raamat: Molecular Chaperones in Human Disorders

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Molecular Chaperones in Human Disorders, Volume 114 in the Advances in Protein Chemistry and Structural Biology series, provides an overview of current developments in mechanisms underlying DNA repair and their involvement in maintaining chromatin repair, the balance between chromosomal repair pathways, tumorigenesis, immune signaling and infection-induced inflammation. Chapters in this new release cover Functional principles and regulation of molecular chaperones, Chaperones and retinal disorders, Protein misfolding and degradation in genetic diseases, Chaperone dysfunction in hereditary myopathic diseases, Diseases caused by functional disorder of molecular chaperones residing in the endoplasmic reticulum, and many other timely topics.

  • Describes advances in our understanding on DNA repair mechanisms and the involvement of their dysregulation in promoting diseases
  • Provides an ideal resource for a very wide audience of specialists, researchers and students
  • Contains timely chapters written by well-renown authorities in their field
  • Presents information that is well supported by a number of high quality illustrations, figures and tables
Contributors xi
Preface xv
1 Functional principles and regulation of molecular chaperones 1(60)
Vinay Dahiya
Johannes Buchner
1 Protein folding
2(1)
2 The concept of molecular chaperones
3(38)
References
41(20)
2 Protein stability and degradation in health and disease 61(24)
Lene Clausen
Amanda B. Abildgaard
Sarah K. Gersing
Amelie Stein
Kresten Lindorff-Larsen
Rasmus Hartmann-Petersen
1 Introduction
62(1)
2 Protein quality control
63(1)
3 The UPS in protein quality control
64(2)
4 Protein quality control in cellular compartments
66(2)
5 Degradation signals
68(2)
6 The consequence of missense mutations for protein stability
70(3)
7 The role of chaperones in protein evolution and manifestation of genetic disorders
73(2)
8 The protein quality control pathway as a drug target for protein conformational diseases
75(1)
9 Concluding remarks
76(1)
Competing interests
77(1)
Funding
77(1)
References
77(8)
3 Chaperones and retinal disorders 85(34)
Maxim Sokolov
Ravi P. Yadav
Celine Brooks
Nikolai O. Artemyev
1 Introduction
86(2)
2 Folding and assembly of transducin βγ: The role of chaperonin
88(4)
3 CCT and the assembly of the BBSome
92(1)
4 Does transducin α require a chaperone?
93(3)
5 AIPL1 is a specialized chaperone of PDE6
96(4)
6 UNC119 and PDE6D as trafficking chaperones of transducin and PDE6
100(6)
7 Outlook
106(1)
Acknowledgment
106(1)
References
106(13)
4 Structural and functional insights on the roles of molecular chaperones in the mistargeting and aggregation phenotypes associated with primary hyperoxaluria type I 119(34)
Jose Angel Fernandez-Higuero
Isabel Betancor-Fernandez
Noel Mesa-Torres
Arturo Muga
Eduardo Salido
Angel L. Pey
1 Molecular chaperones in protein homeostasis
120(11)
2 Primary hyperoxaluria type I (PH1): A LOF disease associated with peroxisomal aggregation and mitochondrial mistargeting
131(9)
3 Small molecule correction of protein homeostasis defects in PH1: Pyridoxine responsiveness and modulators of protein homeostasis and mitochondrial import
140(1)
4 Outlook and future directions
141(2)
Acknowledgments
143(1)
References
143(10)
5 Inflammatory response and its relation to sphingolipid metabolism proteins: Chaperones as potential indirect anti-inflammatory agents 153(68)
Z. Begum Yagci
Elif Esvap
Hatice Asuman Ozkara
Kutlu O. Ulgen
Elif Ozkirimli Olmez
1 Introduction
155(4)
2 Inflammation
159(4)
3 Sphingolipid metabolism
163(3)
4 Sphingolipids involved in inflammation
166(7)
5 Protein-protein interaction network for the crosstalk between inflammation and sphingolipid metabolism
173(4)
6 Neuroinflammation, inflammatory diseases and sphingolipids
177(4)
7 Inherited disorders of lysosomal sphingolipid metabolism: Sphingolipidoses
181(6)
8 Sphingolipidoses and inflammation
187(10)
9 Conclusions and future perspectives
197(4)
Acknowledgments
201(1)
References
201(20)
6 When safeguarding goes wrong: Impact of oxidative stress on protein homeostasis in health and neurodegenerative disorders 221(44)
Ravit Mesika
Dana Reichmann
1 Introduction
222(1)
2 Cellular oxidants: Origin, targets, and benefits
223(4)
3 How do cells overcome oxidative stress and protect their proteome?
227(9)
4 Global transcription factors mediate the oxidative stress response
236(2)
5 The crosstalk between proteostasis and redox homeostasis in age-associated neurodegenerative disorders (NDs)
238(12)
6 Modulating protein homeostasis to treat neurodegenerative diseases
250(1)
References
251(14)
7 The roles of cytosolic quality control proteins, SGTA and the BAG6 complex, in disease 265(50)
Rashi Benarroch
Jennifer M. Austin
Fahmeda Ahmed
Rivka L. Isaacson
1 Introduction
266(1)
2 Hydrophobic parts of proteins exposed to the cytoplasm pose an aggregation risk
267(1)
3 The specific case of tail-anchored proteins
268(1)
4 Triage and fate of hydrophobic substrates in the cytoplasm
268(2)
5 SGTA
270(1)
6 SGTA structure
270(2)
7 Regulation of cytosolic quality control by SGTA
272(1)
8 Role of SGTA in neurodegenerative diseases
273(1)
9 The androgen signaling pathway and SGTA
274(1)
10 The role of SGTA in prostate cancer
274(1)
11 The role of SGTA in polycystic ovary syndrome
275(1)
12 The role of SGTA in breast cancer
276(1)
13 SGTA in the cell cycle
276(1)
14 The role of SGTA in lung cancer
277(1)
15 The role of SGTA in esophageal cancer
277(1)
16 Early identifications of SGTA in viral infections
278(1)
17 SGTA and the simian virus 40
278(1)
18 BAG6
279(1)
19 BAG6 structure
280(1)
20 BAG6 structure: N-Terminal UBL domain
281(1)
21 BAG6 structure: C-Terminal BAG domain
282(1)
22 BAG6 structure: NLS domain
283(1)
23 BAG6 is an essential apoptotic regulator of nascent polypeptides
284(1)
24 BAG6 involved in the triage system during protein quality control
285(1)
25 BAG6 coupled degradation of defective nascent polypeptides
285(3)
26 BAG6 complex-Structural interaction with UBL4A
288(1)
27 BAG6 associations with disease
289(1)
28 The role of BAG6 in male infertility
289(1)
29 The role of BAG6 in lung cancer
290(1)
30 The role of BAG6 in osteoarthritis
290(1)
31 The role of BAG6 in autoimmune disease
291(1)
32 BAG6: future prospects
292(1)
33 Other members of the BAG6 complex and machinery for TA protein insertion
292(2)
34 Formation of the Get4/5 and cBag6 complex
294(1)
35 Structures and binding domains of proteins in the Get4/5 and the cBag6 complexes
295(2)
36 Protein-protein interactions of the Get4/5 (cBag6) complex in the GET/TRC pathway
297(1)
37 Interaction of Get4/5 (cBag6) complex with Sgt2 (SGTA)
297(2)
38 Interaction of Get4/5 (cBag6) complex with Get3 (TRC40)
299(2)
39 Protein interactions in the TRC(GET) pathway
301(1)
40 Disease related to this quality control system
302(2)
41 Disease seemingly unrelated to the chaperone system
304(1)
42 Conclusion
305(1)
References
305(10)
8 A comparative computational approach toward pharmacological chaperones (NN-DNJ and ambroxol) on N3705 and L444P mutations causing Gaucher's disease 315(26)
D. Thirumal Kumar
Sharada Iyer
J. Priyadharshini Christy
R. Siva
Iftikhar Aslam Tayubi
C. George Priya Doss
Hatem Zayed
1 Introduction
316(2)
2 Materials and methods
318(2)
3 Results
320(12)
4 Discussion
332(3)
5 Conclusion
335(1)
Acknowledgments
335(1)
Disclosure statement
335(1)
References
335(4)
Further reading
339(2)
9 Computational and modeling approaches to understand the impact of the Fabry's disease causing mutation (D92Y) on the interaction with pharmacological chaperone 1-deoxygalactonojirimycin (DGJ) 341
D. Thirumal Kumar
E. Judith
J. Priyadharshini Christy
R. Siva
Iftikhar Aslam Tayubi
Chiranjib Chakraborty
C. George Priya Doss
Hatem Zayed
1 Introduction
342(2)
2 Methods and materials
344(2)
3 Results
346(55)
4 Discussion
401(3)
5 Conclusion
404(1)
Acknowledgments
404(1)
Disclosure statement
404(1)
References
405
Rossen Donev received his PhD degree in 1999 from the Institute of Molecular Biology, Bulgarian Academy of Sciences. He did postdoctoral training at Imperial Cancer Research Fund, UK (renamed after the merger with Cancer Research Campaign to Cancer Research UK, London Research Institute) and Cardiff University. In 2007 he was awarded a New Investigator Grant Award from the Medical Research Council (UK) to establish himself as an independent Principle Investigator. In 2010 Dr. Donev was appointed Senior Lecturer at Swansea University. In 2016 Dr. Donev joined MicroPharm Ltd (UK) where currently he is Head of Research. He has published more than 60 research papers, chaired scientific meetings and given invited plenary talks. Rossen Donev has consulted on projects related to development of treatments for neurodevelopmental disorders and cancer therapies. He serves as Editor-in-Chief of the Advances in Protein Chemistry and Structural Biology and on editorial board of several other journals. His research interests include signaling pathways involved in neuropsychiatric disorders and tumor escape from the immune system, and development of therapeutic strategies for their treatment. More recently he has focused on development of immunotherapeutics for non-systemic applications.
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