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  1. Article ; Online: Tertiary structure and conformational dynamics of the anti-amyloidogenic chaperone DNAJB6b at atomistic resolution.

    Adupa, Vasista / Ustyantseva, Elizaveta / Kampinga, Harm H / Onck, Patrick R

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 3285

    Abstract: DNAJB6b is a molecular chaperone of the heat shock protein network, shown to play a crucial role in preventing aggregation of several disease-related intrinsically disordered proteins. Using homology modeling and microsecond-long all-atom molecular ... ...

    Abstract DNAJB6b is a molecular chaperone of the heat shock protein network, shown to play a crucial role in preventing aggregation of several disease-related intrinsically disordered proteins. Using homology modeling and microsecond-long all-atom molecular dynamics (MD) simulations, we show that monomeric DNAJB6b is a transiently interconverting protein cycling between three states: a closed state, an open state (both abundant), and a less abundant extended state. Interestingly, the reported regulatory autoinhibitory anchor between helix V in the G/F
    MeSH term(s) Humans ; Molecular Chaperones/metabolism ; HSP70 Heat-Shock Proteins/metabolism ; Heat-Shock Proteins/metabolism ; Molecular Dynamics Simulation ; Molecular Conformation ; Muscular Dystrophies, Limb-Girdle ; HSP40 Heat-Shock Proteins/metabolism
    Chemical Substances Molecular Chaperones ; HSP70 Heat-Shock Proteins ; Heat-Shock Proteins ; HSP40 Heat-Shock Proteins
    Language English
    Publishing date 2024-04-16
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-46587-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Oxidative stress monitoring in iPSC-derived motor neurons using genetically encoded biosensors of H

    Ustyantseva, Elizaveta / Pavlova, Sophia V / Malakhova, Anastasia A / Ustyantsev, Kirill / Zakian, Suren M / Medvedev, Sergey P

    Scientific reports

    2022  Volume 12, Issue 1, Page(s) 8928

    Abstract: Oxidative stress plays an important role in the development of neurodegenerative diseases, being either the initiator or part of a pathological cascade that leads to the neuron's death. Genetically encoded biosensors of oxidative stress demonstrated ... ...

    Abstract Oxidative stress plays an important role in the development of neurodegenerative diseases, being either the initiator or part of a pathological cascade that leads to the neuron's death. Genetically encoded biosensors of oxidative stress demonstrated their general functionality and overall safety in various systems. However, there is still insufficient data regarding their use in the research of disease-related phenotypes in relevant model systems, such as human cells. Here, we establish an approach for monitoring the redox state of live motor neurons with SOD1 mutations associated with amyotrophic lateral sclerosis. Using CRISPR/Cas9, we insert genetically encoded biosensors of cytoplasmic and mitochondrial H
    MeSH term(s) Biosensing Techniques ; Hydrogen Peroxide/metabolism ; Hydrogen Peroxide/pharmacology ; Induced Pluripotent Stem Cells/metabolism ; Motor Neurons/metabolism ; Oxidative Stress
    Chemical Substances Hydrogen Peroxide (BBX060AN9V)
    Language English
    Publishing date 2022-05-27
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-022-12807-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: DNAJB8 oligomerization is mediated by an aromatic-rich motif that is dispensable for substrate activity.

    Ryder, Bryan D / Ustyantseva, Elizaveta / Boyer, David R / Mendoza-Oliva, Ayde / Kuska, Mikolaj / Wydorski, Pawel M / Macierzynska, Paulina / Morgan, Nabil / Sawaya, Michael R / Diamond, Marc I / Kampinga, Harm H / Joachimiak, Lukasz

    bioRxiv : the preprint server for biology

    2024  

    Abstract: J-domain protein (JDP) molecular chaperones have emerged as central players that maintain a healthy proteome. The diverse members of the JDP family function as monomers/dimers and a small subset assemble into micron-sized oligomers. The oligomeric JDP ... ...

    Abstract J-domain protein (JDP) molecular chaperones have emerged as central players that maintain a healthy proteome. The diverse members of the JDP family function as monomers/dimers and a small subset assemble into micron-sized oligomers. The oligomeric JDP members have eluded structural characterization due to their low-complexity, intrinsically disordered middle domains. This in turn, obscures the biological significance of these larger oligomers in protein folding processes. Here, we identified a short, aromatic motif within DNAJB8, that drives self-assembly through pi-pi stacking and determined its X-ray structure. We show that mutations in the motif disrupt DNAJB8 oligomerization in vitro and in cells. DNAJB8 variants that are unable to assemble bind to misfolded tau seeds more specifically and retain capacity to reduce protein aggregation in vitro and in cells. We propose a new model for DNAJB8 function in which the sequences in the low-complexity domains play distinct roles in assembly and substrate activity.
    Language English
    Publishing date 2024-01-23
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.03.06.531355
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: DNAJB8 oligomerization is mediated by an aromatic-rich motif that is dispensable for substrate activity.

    Ryder, Bryan D / Ustyantseva, Elizaveta / Boyer, David R / Mendoza-Oliva, Ayde / Kuska, Mikołaj I / Wydorski, Paweł M / Macierzyńska, Paulina / Morgan, Nabil / Sawaya, Michael R / Diamond, Marc I / Kampinga, Harm H / Joachimiak, Lukasz A

    Structure (London, England : 1993)

    2024  

    Abstract: J-domain protein (JDP) molecular chaperones have emerged as central players that maintain a healthy proteome. The diverse members of the JDP family function as monomers/dimers and a small subset assemble into micron-sized oligomers. The oligomeric JDP ... ...

    Abstract J-domain protein (JDP) molecular chaperones have emerged as central players that maintain a healthy proteome. The diverse members of the JDP family function as monomers/dimers and a small subset assemble into micron-sized oligomers. The oligomeric JDP members have eluded structural characterization due to their low-complexity, intrinsically disordered middle domains. This in turn, obscures the biological significance of these larger oligomers in protein folding processes. Here, we identified a short, aromatic motif within DNAJB8 that drives self-assembly through π-π stacking and determined its X-ray structure. We show that mutations in the motif disrupt DNAJB8 oligomerization in vitro and in cells. DNAJB8 variants that are unable to assemble bind to misfolded tau seeds more specifically and retain capacity to reduce protein aggregation in vitro and in cells. We propose a new model for DNAJB8 function in which the sequences in the low-complexity domains play distinct roles in assembly and substrate activity.
    Language English
    Publishing date 2024-03-08
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2024.02.015
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4141: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
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  5. Article ; Online: J-domain proteins: From molecular mechanisms to diseases.

    Marszalek, Jaroslaw / De Los Rios, Paolo / Cyr, Douglas / Mayer, Matthias P / Adupa, Vasista / Andréasson, Claes / Blatch, Gregory L / Braun, Janice E A / Brodsky, Jeffrey L / Bukau, Bernd / Chapple, J Paul / Conz, Charlotte / Dementin, Sébastien / Genevaux, Pierre / Genest, Olivier / Goloubinoff, Pierre / Gestwicki, Jason / Hammond, Colin M / Hines, Justin K /
    Ishikawa, Koji / Joachimiak, Lukasz A / Kirstein, Janine / Liberek, Krzysztof / Mokranjac, Dejana / Nillegoda, Nadinath / Ramos, Carlos H I / Rebeaud, Mathieu / Ron, David / Rospert, Sabine / Sahi, Chandan / Shalgi, Reut / Tomiczek, Bartlomiej / Ushioda, Ryo / Ustyantseva, Elizaveta / Ye, Yihong / Zylicz, Maciej / Kampinga, Harm H

    Cell stress & chaperones

    2023  Volume 29, Issue 1, Page(s) 21–33

    Abstract: J-domain proteins (JDPs) are the largest family of chaperones in most organisms, but much of how they function within the network of other chaperones and protein quality control machineries is still an enigma. Here, we report on the latest findings ... ...

    Abstract J-domain proteins (JDPs) are the largest family of chaperones in most organisms, but much of how they function within the network of other chaperones and protein quality control machineries is still an enigma. Here, we report on the latest findings related to JDP functions presented at a dedicated JDP workshop in Gdansk, Poland. The report does not include all (details) of what was shared and discussed at the meeting, because some of these original data have not yet been accepted for publication elsewhere or represented still preliminary observations at the time.
    MeSH term(s) HSP70 Heat-Shock Proteins/metabolism ; Molecular Chaperones/metabolism ; Poland ; HSP40 Heat-Shock Proteins/metabolism
    Chemical Substances HSP70 Heat-Shock Proteins ; Molecular Chaperones ; HSP40 Heat-Shock Proteins
    Language English
    Publishing date 2023-12-23
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1362749-1
    ISSN 1466-1268 ; 1355-8145
    ISSN (online) 1466-1268
    ISSN 1355-8145
    DOI 10.1016/j.cstres.2023.12.002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4797: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

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