Atjaunināt sīkdatņu piekrišanu

E-grāmata: Dancing Protein Clouds: Intrinsically Disordered Proteins in the Norm and Pathology, Part C

Volume editor (Department of Molecular Medicine and USF Health Byrd Alzheimers Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, United States)
Citas grāmatas par šo tēmu:
  • Formāts - EPUB+DRM
  • Cena: 156,48 €*
  • * ši ir gala cena, t.i., netiek piemērotas nekādas papildus atlaides
  • Ielikt grozā
  • Pievienot vēlmju sarakstam
  • Šī e-grāmata paredzēta tikai personīgai lietošanai. E-grāmatas nav iespējams atgriezt un nauda par iegādātajām e-grāmatām netiek atmaksāta.
Dancing Protein Clouds: Intrinsically Disordered Proteins in the Norm and Pathology, Part CPalielināt
Citas grāmatas par šo tēmu:

DRM restrictions

  • Kopēšana (kopēt/ievietot):

    nav atļauts

  • Drukāšana:

    nav atļauts

  • Lietošana:

    Digitālo tiesību pārvaldība (Digital Rights Management (DRM))
    Izdevējs ir piegādājis šo grāmatu šifrētā veidā, kas nozīmē, ka jums ir jāinstalē bezmaksas programmatūra, lai to atbloķētu un lasītu. Lai lasītu šo e-grāmatu, jums ir jāizveido Adobe ID. Vairāk informācijas šeit. E-grāmatu var lasīt un lejupielādēt līdz 6 ierīcēm (vienam lietotājam ar vienu un to pašu Adobe ID).

    Nepieciešamā programmatūra
    Lai lasītu šo e-grāmatu mobilajā ierīcē (tālrunī vai planšetdatorā), jums būs jāinstalē šī bezmaksas lietotne: PocketBook Reader (iOS / Android)

    Lai lejupielādētu un lasītu šo e-grāmatu datorā vai Mac datorā, jums ir nepieciešamid Adobe Digital Editions (šī ir bezmaksas lietotne, kas īpaši izstrādāta e-grāmatām. Tā nav tas pats, kas Adobe Reader, kas, iespējams, jau ir jūsu datorā.)

    Jūs nevarat lasīt šo e-grāmatu, izmantojot Amazon Kindle.

Dancing Protein Clouds: Intrinsically Disordered Proteins in the Norm and Pathology, Part C, Volume 183 represents a set of selected studies on a variety of research topics related to intrinsically disordered proteins. Topics in this volume include discussions on the evolution of disorder, consideration of the peculiarities of phase separation of the prion protein, a general discussion of the relationships between intrinsic disorder and protein functions, coverage of the structural and functional characterization of several important intrinsically disordered proteins, such as transcription factors, outer membrane porins, trans-membrane and membrane associated proteins with ID regions, discussion of molecular simulations of IDPs, and much more.

  • Provides recent studies on the intrinsically disordered proteins and their functions, along with the involvement of intrinsically disordered proteins in the pathogenesis of various diseases
  • Contains numerous illustrative materials (color figures, diagrams and tables) to help readers delve into the information provided
  • Includes contributions from recognized experts in the field
Contributors ix
Preface: The Patchwork Quilt of Intrinsic Disorder xiii
1 Intrinsic disorder and phase transitions: Pieces in the puzzling role of the prion protein in health and disease
1(44)
Mariana J. do Amaral
Yraima Cordeiro
1 Introduction
2(6)
2 Considerations on intrinsic disorder and phase separation ability of the prion protein family
8(6)
3 The manifold interactions of PrP with nucleic acid targets: Can phase separation explain it?
14(10)
4 Phase transitions of PrP in health and disease
24(21)
Acknowledgments
32(1)
References
32(13)
2 Functions of intrinsically disordered proteins through evolutionary lenses
45(30)
Matyas Pajkos
Zsuzsanna Dosztanyi
1 Introduction
46(1)
2 Functional categories of IDPs
47(8)
3 Distinct evolutionary scenarios of IDRs
55(8)
4 Evolutionary conservation of SLIMs
63(3)
5 Evolutionary origin IDRs mutated in cancer
66(2)
6 Conclusion
68(7)
References
69(6)
3 Non-specific porins of Gram-negative bacteria as proteins containing intrinsically disordered regions with amyloidogenic potential
75(26)
Olga D. Novikova
Vladimir N. Uversky
Elena A. Zelepuga
Funding
96(1)
Acknowledgment
96(1)
References
96(5)
4 Intrinsic disorder in integral membrane proteins
101(34)
Brian J. Aneskievich
Rambon Shamilov
Olga Vinogradova
1 Distinction between intrinsically disordered and structured proteins
102(4)
2 Intrinsic disorder in IMPs: Potential functional advantages
106(12)
3 Mutations in IMP: Consideration of IDR
118(4)
4 IMP intrinsic disorder: Investigational approaches
122(5)
5 Conclusions
127(8)
References
128(7)
5 Molecular simulations of IDPs: From ensemble generation to IDP interactions leading to disorder-to-order transitions
135(52)
Hebah Fatafta
Suman Samantray
Abdallah Sayyed-Ahmad
Orkid Coskuner-Weber
Birgit Strodel
1 Introduction to IDPs
136(13)
2 Force fields for IDPs
149(8)
3 Simulation-based IDP ensemble generation and characterization
157(9)
4 Modeling the disorder-to-order transition of IDPs
166(7)
5 Summary and outlook
173(14)
Acknowledgments
174(1)
References
174(13)
6 Target-binding behavior of IDPs via pre-structured motifs
187(62)
Do-Hyoung Kim
Kyou-Hoon Han
1 Introduction
189(1)
2 Target-binding of IDPs
190(6)
3 The pre-structured motif (PreSMo)
196(10)
4 PreSMos in transcriptional and translational factors
206(16)
5 PreSMos in neurodegenerative IDPs
222(6)
6 PreSMos in other IDPs
228(5)
7 Summary and perspective
233(16)
Acknowledgments
235(1)
References
235(14)
7 The role of dancing duplexes in biology and disease
249(22)
Heather M. Forsythe
Elisar Barbar
1 Introduction
250(1)
2 LC8-facilitated dimerization in IDP duplexes
250(5)
3 Multivalent binding of LC8 along IDP duplexes
255(5)
4 Nupl 59: A multivalent LC8 binder with a self-association domain
260(1)
5 VSV-P: The role of disorder in a non-LC8 binding IDP duplex
261(1)
6 The role of disorder and dimerization of the SARS-CoV-2 nucleocapsid phosphoprotein IDP duplex
262(3)
7 Future directions
265(2)
8 Conclusion
267(4)
Acknowledgments
267(1)
References
267(4)
8 Intrinsic disorder in protein kinase A anchoring proteins signaling complexes
271(24)
Mateusz Dyla
Magnus Kjaergaard
1 Tethered phosphorylation
273(2)
2 Intrinsic disorder in PKA-AKAP signaling complexes
275(2)
3 The prevalence of intrinsic disorder in AKAPs
277(7)
4 Modeling the reach and effective concentration of PKA-AKAP signaling complexes
284(4)
5 Allosteric regulation of tethered reactions by AKAP structure
288(3)
6 Conclusions
291(4)
References
291(4)
9 Protein intrinsic disorder on a dynamic nucleosomal landscape
295(60)
Sveinn Bjarnason
Sarah F. Ruidiaz
Jordan Mclvor
Davide Mercadante
Petur O. Heidarsson
1 Introduction
296(1)
2 Protein intrinsic disorder on a nucleosomal landscape
297(10)
3 Disordered interactions with nucleosomes
307(29)
4 Common sequence features of disordered nucleosome-binding proteins
336(3)
5 Concluding remarks
339(16)
Acknowledgments
340(1)
References
340(15)
10 Flexible spandrels of the global plant virome: Proteomic-wide evolutionary patterns of structural intrinsic protein disorder elucidate modulation at the functional virus-host interplay
355(56)
Rachid Tahzima
Annelies Haegeman
Sebastien Massart
Eugenie Hebrard
1 The highly modular plant virus proteome
357(6)
2 Protein disorder composition in plant viruses: Terra incognita
363(3)
3 The global plant virus proteome reveals overhauling IDP abundance and variability
366(4)
4 General affinity of phylogenomically unrelated small plant virus proteomes with increased IDP
370(1)
5 Emerging patterns in amino acid composition as a potential predictor of IDP and virus functional biology
371(7)
6 The global plant virus MoRFome: Gaining functional insights in viral IDP-mediated binding contextual landscape via harnessing interface molecular recognition features
378(3)
7 Evolutionary proteomic comparative analysis of conserved viral modules make up reveals IDP landscape of viral-host interacting disordomes
381(5)
8 Functional IDP and evolutionary conserved structures expand evidence for modulation of transmission mode of plant viruses by insect vectors
386(4)
9 Outlook and new challenging prospects for plant virology
390(10)
10 Conclusion
400(11)
References
400(8)
Further Reading
408(3)
Index 411
Prof. Vladimir N. Uversky, PhD, DSc, FRSB, FRSC, F.A.I.M.B.E., Professor at the Department of Molecular Medicine, Morsani College of Medicine, University of South Florida (USF), is a pioneer in the field of protein intrinsic disorder. He has made a number of groundbreaking contributions in the field of protein folding, misfolding, and intrinsic disorder. He obtained his PhD from Moscow Institute of Physics and Technology and D.Sc. from the Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences. Since 2010, Professor Uversky has worked at University of South Florida, where he works on various aspects of protein intrinsic disorder phenomenon and analysis of protein folding and misfolding processes. He has authored over 1250 scientific publications and edited several books and book series on protein structure, function, folding, misfolding, and intrinsic disorder. He also servs as an editor in a number of scientific journals.
Biežāk uzdotie jautājumi par e-grāmatām Biežāk uzdotie jautājumi par e-grāmatām
Permanent link: https://www.kriso.lv/db/97803238530026e.html
Keywords: