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  1. Book ; Online: Biological Liquid-Liquid Phase Separation, Biomolecular Condensates, and Membraneless Organelles

    Uversky, Vladimir N

    2023  

    Keywords Research & information: general ; Biology, life sciences ; Alzheimer's disease ; amyloid aggregation ; lipid bilayer ; cholesterol ; time-lapse AFM imaging ; molecular dynamics ; liquid-liquid phase separation (LLPS) ; membraneless organelles ; phase-separated condensates ; human diseases ; liquid-liquid phase separation ; intrinsically disordered proteins ; proteins with low complexity ; P-body ; Nst1 ; polyampholyte domain ; aggregation-prone domain ; Saccharomyces cerevisiae ; membrane-less organelle ; nuclear speckle ; nucleolus ; phase separation ; chromatin organization ; nuclear condensate ; intrinsically disordered region ; transcription ; DNA damage repair ; super-enhancer ; quantitative imaging ; CTP synthase ; cytoophidium ; fluorescence recovery after photobleaching (FRAP) ; stimulated emission depletion (STED) ; Drosophila ; epithelium ; follicle cell ; ingression ; paramyxoviruses ; Hendra virus ; amyloid-like fibrils ; Taylor Dispersion Analysis (TDA) ; negative staining Transmission Electron Microscopy (ns-TEM) ; Polyethylene glycol (PEG) precipitation assays ; Congo Red ; Small-Angle X-ray Scattering (SAXS) ; actin ; actin polymerization ; actin-binding proteins ; coacervate ; membrane ; signaling proteins ; n/a
    Language English
    Size 1 electronic resource (202 pages)
    Publisher MDPI - Multidisciplinary Digital Publishing Institute
    Publishing place Basel
    Document type Book ; Online
    Note English
    HBZ-ID HT030646166
    ISBN 9783036589305 ; 3036589309
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Book ; Online ; E-Book: Droplets of life

    Uversky, Vladimir N.

    membrane-less organelles, biomolecular condensates, and biological liquid-liquid phase separation

    2023  

    Author's details Vladimir Uversky
    Keywords Cell organelles
    Subject code 574.8734
    Language English
    Size 1 online resource (730 pages)
    Publisher Academic Press
    Publishing place London
    Document type Book ; Online ; E-Book
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    ISBN 0-12-824175-6 ; 9780128239674 ; 978-0-12-824175-2 ; 0128239670
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  3. Book ; Online ; E-Book: Structure and intrinsic disorder in enzymology

    Uversky, Vladimir N. / Gupta, Munishwar Nath

    (Foundations and frontiers in enzymology)

    2023  

    Author's details edited by Munishwar Nath Gupta, Vladimir N. Uversky
    Series title Foundations and frontiers in enzymology
    Keywords Enzymes. ; Enzymes/Structure
    Subject code 574.1925
    Language English
    Size 1 online resource (529 pages)
    Publisher Academic Press, an imprint of Elsevier
    Publishing place London
    Document type Book ; Online ; E-Book
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    ISBN 0-323-99534-9 ; 9780323995337 ; 978-0-323-99534-4 ; 0323995330
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  4. Book ; Online: Intrinsically Disordered Proteins and Chronic Diseases

    Kulkarni, Prakash / Uversky, Vladimir N.

    2021  

    Keywords Research & information: general ; IDP ; fuzzy interactions ; protein complementation assays ; split-GFP reassembly ; kinetics ; membraneless organelles ; optical tweezer ; liquid-liquid phase separation ; protein diffusion ; depletion interaction ; entropic force ; low-complexity sequences ; intrinsically disordered proteins ; PAGE4 ; conformational plasticity ; order-disorder transition ; phosphorylation ; intrinsic disordered protein ; extremely fuzzy complex ; protein interaction ; binding mechanism ; tumor protein p53 ; mouse double minute 2 ; mouse double minute 4 ; Kinase-inducible domain interacting domain ; phosphomimetics ; nuclear magnetic resonance ; transient secondary structure ; COR15A ; Late embryogenesis abundant ; Trifluoroethanol ; Nuclear magnetic resonance ; intrinsically disordered regions ; functional segments ; disease-related proteins ; protein-protein interaction ; subcellular location ; glucocorticoid receptor ; intrinsically disordered ; transactivation activity ; gene regulation ; coactivators ; microtubule associated protein ; tau ; intrinsically disordered protein ; dynamic configuration ; free energy landscape ; microtubules ; electrostatics ; diffusion ; protein structure prediction ; molecular modelling ; molecular dynamics ; tau-microtubule association ; conformational ensemble ; replica exchange molecular dynamics ; drug design ; n/a
    Size 1 electronic resource (224 pages)
    Publisher MDPI - Multidisciplinary Digital Publishing Institute
    Publishing place Basel, Switzerland
    Document type Book ; Online
    Note English ; Open Access
    HBZ-ID HT021291634
    ISBN 9783036512631 ; 3036512632
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  5. Article ; Online: Marc H. V. van Regenmortel, a virtual friend and a real colleague.

    Uversky, Vladimir N

    Journal of molecular recognition : JMR

    2024  Volume 37, Issue 3, Page(s) e3079

    MeSH term(s) Humans ; Friends
    Language English
    Publishing date 2024-02-28
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1015084-5
    ISSN 1099-1352 ; 0952-3499
    ISSN (online) 1099-1352
    ISSN 0952-3499
    DOI 10.1002/jmr.3079
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2954: Show issues Location:
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    ab Jg. 2022: Lesesaal (EG)

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  6. Book: Dancing protein clouds / Part C

    Uverskij, Vladimir N.

    intrinsically disordered proteins in health and disease

    (Progress in molecular biology and translational science ; volume 183)

    2021  

    Author's details edited by Vladimir N. Uversky
    Series title Progress in molecular biology and translational science ; volume 183
    Dancing protein clouds
    Collection Dancing protein clouds
    Language English
    Size xviii, 417 Seiten, Illustrationen, Diagramme
    Edition First edition
    Publishing country United States
    Document type Book
    HBZ-ID HT021156616
    ISBN 978-0-323-85299-9 ; 0-323-85299-8
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs 357 -183- Location:
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  7. Book ; Online: Intrinsically disordered proteins and chronic diseases

    Kulkarni, Prakash / Uverskij, Vladimir N.

    2021  

    Author's details Editors: Prakash Kulkarni and Vladimir N. Uverskij
    Language English
    Size 1 Online-Ressource (viii, 214 Seiten), Illustrationen
    Publisher MDPI
    Publishing place Bern
    Publishing country Switzerland
    Document type Book ; Online
    Note special issue, published in "Biomolecules" ; Open Access
    HBZ-ID HT021153181
    ISBN 978-3-0365-1263-1 ; 9783036512624 ; 3-0365-1263-2 ; 3036512624
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  8. Article ; Online: Biological Liquid-Liquid Phase Separation, Biomolecular Condensates, and Membraneless Organelles: Now You See Me, Now You Don't.

    Uversky, Vladimir N

    International journal of molecular sciences

    2023  Volume 24, Issue 17

    Abstract: Liquid-liquid phase separation (LLPS, also known as biomolecular condensation) and the related biogenesis of various membraneless organelles (MLOs) and biomolecular condensates (BMCs) are now considered fundamental molecular mechanisms governing the ... ...

    Abstract Liquid-liquid phase separation (LLPS, also known as biomolecular condensation) and the related biogenesis of various membraneless organelles (MLOs) and biomolecular condensates (BMCs) are now considered fundamental molecular mechanisms governing the spatiotemporal organization of the intracellular space [...].
    MeSH term(s) Biomolecular Condensates ; Intracellular Space
    Language English
    Publishing date 2023-08-24
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms241713150
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Functional unfoldomics: Roles of intrinsic disorder in protein (multi)functionality.

    Uversky, Vladimir N

    Advances in protein chemistry and structural biology

    2023  Volume 138, Page(s) 179–210

    Abstract: Intrinsically disordered proteins (IDPs), which are functional proteins without stable tertiary structure, and hybrid proteins containing ordered domains and intrinsically disordered regions (IDRs) constitute prominent parts of all proteomes collectively ...

    Abstract Intrinsically disordered proteins (IDPs), which are functional proteins without stable tertiary structure, and hybrid proteins containing ordered domains and intrinsically disordered regions (IDRs) constitute prominent parts of all proteomes collectively known as unfoldomes. IDPs/IDRs exist as highly dynamic structural ensembles of rapidly interconverting conformations and are characterized by the exceptional structural heterogeneity, where their different parts are (dis)ordered to different degree, and their overall structure represents a complex mosaic of foldons, inducible foldons, inducible morphing foldons, non-foldons, semifoldons, and even unfoldons. Despite their lack of unique 3D structures, IDPs/IDRs play crucial roles in the control of various biological processes and the regulation of different cellular pathways and are commonly involved in recognition and signaling, indicating that the disorder-based functional repertoire is complementary to the functions of ordered proteins. Furthermore, IDPs/IDRs are frequently multifunctional, and this multifunctionality is defined by their structural flexibility and heterogeneity. Intrinsic disorder phenomenon is at the roots of the structure-function continuum model, where the structure continuum is defined by the presence of differently (dis)ordered regions, and the function continuum arises from the ability of all these differently (dis)ordered parts to have different functions. In their everyday life, IDPs/IDRs utilize a broad spectrum of interaction mechanisms thereby acting as interaction specialists. They are crucial for the biogenesis of numerous proteinaceous membrane-less organelles driven by the liquid-liquid phase separation. This review introduces functional unfoldomics by representing some aspects of the intrinsic disorder-based functionality.
    MeSH term(s) Protein Conformation ; Models, Molecular ; Intrinsically Disordered Proteins/metabolism ; Signal Transduction ; Proteome
    Chemical Substances Intrinsically Disordered Proteins ; Proteome
    Language English
    Publishing date 2023-11-22
    Publishing country Netherlands
    Document type Review ; Journal Article
    ZDB-ID 2473077-4
    ISSN 1876-1631 ; 1876-1623
    ISSN (online) 1876-1631
    ISSN 1876-1623
    DOI 10.1016/bs.apcsb.2023.11.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  10. Article ; Online: Rebellion of the deregulated regulators: What is the clinical relevance of studying intrinsically disordered proteins?

    Uversky, Vladimir N

    Expert review of proteomics

    2023  Volume 19, Issue 7-12, Page(s) 279–282

    MeSH term(s) Humans ; Intrinsically Disordered Proteins/genetics ; Intrinsically Disordered Proteins/metabolism ; Clinical Relevance ; Protein Conformation ; Organelles/metabolism
    Chemical Substances Intrinsically Disordered Proteins
    Language English
    Publishing date 2023-02-06
    Publishing country England
    Document type Editorial
    ZDB-ID 2299100-1
    ISSN 1744-8387 ; 1478-9450
    ISSN (online) 1744-8387
    ISSN 1478-9450
    DOI 10.1080/14789450.2023.2176755
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6686: Show issues Location:
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