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  1. Article ; Online: Confined Catalytic Janus Swimmers in a Crowded Channel: Geometry-Driven Rectification Transients and Directional Locking.

    Yu, Hailing / Kopach, Andrii / Misko, Vyacheslav R / Vasylenko, Anna A / Makarov, Denys / Marchesoni, Fabio / Nori, Franco / Baraban, Larysa / Cuniberti, Gianaurelio

    Small (Weinheim an der Bergstrasse, Germany)

    2016  Volume 12, Issue 42, Page(s) 5882–5890

    Abstract: Self-propelled Janus particles, acting as microscopic vehicles, have the potential to perform complex tasks on a microscopic scale, suitable, e.g., for environmental applications, on-chip chemical information processing, or in vivo drug delivery. ... ...

    Abstract Self-propelled Janus particles, acting as microscopic vehicles, have the potential to perform complex tasks on a microscopic scale, suitable, e.g., for environmental applications, on-chip chemical information processing, or in vivo drug delivery. Development of these smart nanodevices requires a better understanding of how synthetic swimmers move in crowded and confined environments that mimic actual biosystems, e.g., network of blood vessels. Here, the dynamics of self-propelled Janus particles interacting with catalytically passive silica beads in a narrow channel is studied both experimentally and through numerical simulations. Upon varying the area density of the silica beads and the width of the channel, active transport reveals a number of intriguing properties, which range from distinct bulk and boundary-free diffusivity at low densities, to directional "locking" and channel "unclogging" at higher densities, whereby a Janus swimmer is capable of transporting large clusters of passive particles.
    Language English
    Publishing date 2016-09-15
    Publishing country Germany
    Document type Journal Article
    ISSN 1613-6829
    ISSN (online) 1613-6829
    DOI 10.1002/smll.201602039
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: RNA-Induced Conformational Switching and Clustering of G3BP Drive Stress Granule Assembly by Condensation.

    Guillén-Boixet, Jordina / Kopach, Andrii / Holehouse, Alex S / Wittmann, Sina / Jahnel, Marcus / Schlüßler, Raimund / Kim, Kyoohyun / Trussina, Irmela R E A / Wang, Jie / Mateju, Daniel / Poser, Ina / Maharana, Shovamayee / Ruer-Gruß, Martine / Richter, Doris / Zhang, Xiaojie / Chang, Young-Tae / Guck, Jochen / Honigmann, Alf / Mahamid, Julia /
    Hyman, Anthony A / Pappu, Rohit V / Alberti, Simon / Franzmann, Titus M

    Cell

    2020  Volume 181, Issue 2, Page(s) 346–361.e17

    Abstract: Stressed cells shut down translation, release mRNA molecules from polysomes, and form stress granules (SGs) via a network of interactions that involve G3BP. Here we focus on the mechanistic underpinnings of SG assembly. We show that, under non-stress ... ...

    Abstract Stressed cells shut down translation, release mRNA molecules from polysomes, and form stress granules (SGs) via a network of interactions that involve G3BP. Here we focus on the mechanistic underpinnings of SG assembly. We show that, under non-stress conditions, G3BP adopts a compact auto-inhibited state stabilized by electrostatic intramolecular interactions between the intrinsically disordered acidic tracts and the positively charged arginine-rich region. Upon release from polysomes, unfolded mRNAs outcompete G3BP auto-inhibitory interactions, engendering a conformational transition that facilitates clustering of G3BP through protein-RNA interactions. Subsequent physical crosslinking of G3BP clusters drives RNA molecules into networked RNA/protein condensates. We show that G3BP condensates impede RNA entanglement and recruit additional client proteins that promote SG maturation or induce a liquid-to-solid transition that may underlie disease. We propose that condensation coupled to conformational rearrangements and heterotypic multivalent interactions may be a general principle underlying RNP granule assembly.
    MeSH term(s) Carrier Proteins/metabolism ; Cell Line, Tumor ; Cytoplasm/metabolism ; Cytoplasmic Granules/metabolism ; DNA Helicases/metabolism ; HeLa Cells ; Humans ; Nucleic Acid Conformation ; Organelles/metabolism ; Phosphorylation ; Poly-ADP-Ribose Binding Proteins/metabolism ; RNA Helicases/metabolism ; RNA Recognition Motif Proteins/metabolism ; RNA, Messenger/metabolism ; Ribonucleoproteins/metabolism ; Stress, Physiological/genetics
    Chemical Substances Carrier Proteins ; Poly-ADP-Ribose Binding Proteins ; RNA Recognition Motif Proteins ; RNA, Messenger ; Ribonucleoproteins ; DNA Helicases (EC 3.6.4.-) ; G3BP1 protein, human (EC 3.6.4.12) ; RNA Helicases (EC 3.6.4.13)
    Language English
    Publishing date 2020-04-16
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2020.03.049
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1167: Show issues Location:
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  3. Article ; Online: An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function.

    Mateju, Daniel / Franzmann, Titus M / Patel, Avinash / Kopach, Andrii / Boczek, Edgar E / Maharana, Shovamayee / Lee, Hyun O / Carra, Serena / Hyman, Anthony A / Alberti, Simon

    The EMBO journal

    2017  Volume 36, Issue 12, Page(s) 1669–1687

    Abstract: Stress granules (SG) are membrane-less compartments involved in regulating mRNAs during stress. Aberrant forms of SGs have been implicated in age-related diseases, such as amyotrophic lateral sclerosis (ALS), but the molecular events triggering their ... ...

    Abstract Stress granules (SG) are membrane-less compartments involved in regulating mRNAs during stress. Aberrant forms of SGs have been implicated in age-related diseases, such as amyotrophic lateral sclerosis (ALS), but the molecular events triggering their formation are still unknown. Here, we find that misfolded proteins, such as ALS-linked variants of SOD1, specifically accumulate and aggregate within SGs in human cells. This decreases the dynamics of SGs, changes SG composition, and triggers an aberrant liquid-to-solid transition of
    MeSH term(s) Cytoplasmic Granules/metabolism ; Epithelial Cells/physiology ; HeLa Cells ; Humans ; Molecular Chaperones/metabolism ; Superoxide Dismutase-1/metabolism
    Chemical Substances Molecular Chaperones ; SOD1 protein, human ; Superoxide Dismutase-1 (EC 1.15.1.1)
    Language English
    Publishing date 2017-04-04
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.201695957
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1808: Show issues Location:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
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    Zs.MG 100: Show issues

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  4. Article ; Online: G3BPs tether the TSC complex to lysosomes and suppress mTORC1 signaling.

    Prentzell, Mirja Tamara / Rehbein, Ulrike / Cadena Sandoval, Marti / De Meulemeester, Ann-Sofie / Baumeister, Ralf / Brohée, Laura / Berdel, Bianca / Bockwoldt, Mathias / Carroll, Bernadette / Chowdhury, Suvagata Roy / von Deimling, Andreas / Demetriades, Constantinos / Figlia, Gianluca / de Araujo, Mariana Eca Guimaraes / Heberle, Alexander M / Heiland, Ines / Holzwarth, Birgit / Huber, Lukas A / Jaworski, Jacek /
    Kedra, Magdalena / Kern, Katharina / Kopach, Andrii / Korolchuk, Viktor I / van 't Land-Kuper, Ineke / Macias, Matylda / Nellist, Mark / Palm, Wilhelm / Pusch, Stefan / Ramos Pittol, Jose Miguel / Reil, Michèle / Reintjes, Anja / Reuter, Friederike / Sampson, Julian R / Scheldeman, Chloë / Siekierska, Aleksandra / Stefan, Eduard / Teleman, Aurelio A / Thomas, Laura E / Torres-Quesada, Omar / Trump, Saskia / West, Hannah D / de Witte, Peter / Woltering, Sandra / Yordanov, Teodor E / Zmorzynska, Justyna / Opitz, Christiane A / Thedieck, Kathrin

    Cell

    2021  Volume 184, Issue 3, Page(s) 655–674.e27

    Abstract: Ras GTPase-activating protein-binding proteins 1 and 2 (G3BP1 and G3BP2, respectively) are widely recognized as core components of stress granules (SGs). We report that G3BPs reside at the cytoplasmic surface of lysosomes. They act in a non-redundant ... ...

    Abstract Ras GTPase-activating protein-binding proteins 1 and 2 (G3BP1 and G3BP2, respectively) are widely recognized as core components of stress granules (SGs). We report that G3BPs reside at the cytoplasmic surface of lysosomes. They act in a non-redundant manner to anchor the tuberous sclerosis complex (TSC) protein complex to lysosomes and suppress activation of the metabolic master regulator mechanistic target of rapamycin complex 1 (mTORC1) by amino acids and insulin. Like the TSC complex, G3BP1 deficiency elicits phenotypes related to mTORC1 hyperactivity. In the context of tumors, low G3BP1 levels enhance mTORC1-driven breast cancer cell motility and correlate with adverse outcomes in patients. Furthermore, G3bp1 inhibition in zebrafish disturbs neuronal development and function, leading to white matter heterotopia and neuronal hyperactivity. Thus, G3BPs are not only core components of SGs but also a key element of lysosomal TSC-mTORC1 signaling.
    MeSH term(s) Adaptor Proteins, Signal Transducing/metabolism ; Amino Acid Sequence ; Animals ; Breast Neoplasms/metabolism ; Breast Neoplasms/pathology ; Cell Line, Tumor ; Cell Movement/drug effects ; Cytoplasmic Granules/drug effects ; Cytoplasmic Granules/metabolism ; DNA Helicases/chemistry ; DNA Helicases/metabolism ; Evolution, Molecular ; Female ; Humans ; Insulin/pharmacology ; Lysosomal Membrane Proteins/metabolism ; Lysosomes/drug effects ; Lysosomes/metabolism ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Neurons/drug effects ; Neurons/metabolism ; Phenotype ; Poly-ADP-Ribose Binding Proteins/chemistry ; Poly-ADP-Ribose Binding Proteins/metabolism ; RNA Helicases/chemistry ; RNA Helicases/metabolism ; RNA Recognition Motif Proteins/chemistry ; RNA Recognition Motif Proteins/metabolism ; RNA-Binding Proteins/metabolism ; Rats, Wistar ; Signal Transduction/drug effects ; Tuberous Sclerosis/metabolism ; Zebrafish/metabolism ; Rats
    Chemical Substances Adaptor Proteins, Signal Transducing ; G3BP2 protein, human ; Insulin ; Lysosomal Membrane Proteins ; Poly-ADP-Ribose Binding Proteins ; RNA Recognition Motif Proteins ; RNA-Binding Proteins ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; DNA Helicases (EC 3.6.4.-) ; G3BP1 protein, human (EC 3.6.4.12) ; RNA Helicases (EC 3.6.4.13)
    Language English
    Publishing date 2021-01-25
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2020.12.024
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1167: Show issues Location:
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    Zs.MG 58: Show issues

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