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  1. Article ; Online: Particle ID: A Multiplexed Hydrogel Bead Platform for Biomedical Applications.

    Alpsoy, Lokman / Sedeky, Abanoub Selim / Rehbein, Ulrike / Thedieck, Kathrin / Brandstetter, Thomas / Rühe, Jürgen

    ACS applied materials & interfaces

    2023  Volume 15, Issue 48, Page(s) 55346–55357

    Abstract: We present a new platform based on hydrogel beads for multiplex analysis that can be fabricated, barcoded, and functionalized in a single step using a simple microfluidic assembly and a photo-cross-linking process. The beads are generated in a two-phase ... ...

    Abstract We present a new platform based on hydrogel beads for multiplex analysis that can be fabricated, barcoded, and functionalized in a single step using a simple microfluidic assembly and a photo-cross-linking process. The beads are generated in a two-phase flow fluidic system and photo-cross-linking of the polymer in the aqueous phase by C,H insertion cross-linking (CHic). The size and shape of the hydrogel particles can be controlled over a wide range by fluidic parameters. During the fabrication of the beads, they are barcoded by using physical and optical barcoding strategies. Magnetic beads and fluorescent particles, which allow identification of the production batch number, are added simultaneously as desired, resulting in complex, multifunctional beads in a one-step reaction. As an example of biofunctionalization,
    MeSH term(s) Humans ; Hydrogels ; Enzyme-Linked Immunosorbent Assay
    Chemical Substances Hydrogels
    Language English
    Publishing date 2023-11-20
    Publishing country United States
    Document type Journal Article
    ISSN 1944-8252
    ISSN (online) 1944-8252
    DOI 10.1021/acsami.3c12122
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Finding new edges: systems approaches to MTOR signaling.

    Heberle, Alexander Martin / Rehbein, Ulrike / Rodríguez Peiris, Maria / Thedieck, Kathrin

    Biochemical Society transactions

    2021  Volume 49, Issue 1, Page(s) 41–54

    Abstract: Cells have evolved highly intertwined kinase networks to finely tune cellular homeostasis to the environment. The network converging on the mechanistic target of rapamycin (MTOR) kinase constitutes a central hub that integrates metabolic signals and ... ...

    Abstract Cells have evolved highly intertwined kinase networks to finely tune cellular homeostasis to the environment. The network converging on the mechanistic target of rapamycin (MTOR) kinase constitutes a central hub that integrates metabolic signals and adapts cellular metabolism and functions to nutritional changes and stress. Feedforward and feedback loops, crosstalks and a plethora of modulators finely balance MTOR-driven anabolic and catabolic processes. This complexity renders it difficult - if not impossible - to intuitively decipher signaling dynamics and network topology. Over the last two decades, systems approaches have emerged as powerful tools to simulate signaling network dynamics and responses. In this review, we discuss the contribution of systems studies to the discovery of novel edges and modulators in the MTOR network in healthy cells and in disease.
    MeSH term(s) Animals ; Gene Regulatory Networks/physiology ; Homeostasis/physiology ; Humans ; Protein Interaction Maps/physiology ; Signal Transduction/physiology ; Systems Integration ; TOR Serine-Threonine Kinases/metabolism ; TOR Serine-Threonine Kinases/physiology
    Chemical Substances MTOR protein, human (EC 2.7.1.1) ; TOR Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2021-02-05
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 184237-7
    ISSN 1470-8752 ; 0300-5127
    ISSN (online) 1470-8752
    ISSN 0300-5127
    DOI 10.1042/BST20190730
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 944: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
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  3. Article: Breaking the Interface: Efficient Extraction of Magnetic Beads from Nanoliter Droplets for Automated Sequential Immunoassays

    Metzler, Lukas / Rehbein, Ulrike / Schönberg, Jan-Niklas / Brandstetter, Thomas / Thedieck, Kathrin / Rühe, Jürgen

    Analytical chemistry. 2020 June 05, v. 92, no. 15

    2020  

    Abstract: Droplet-based microfluidic systems offer a high potential for miniaturization and automation. Therefore, they are becoming an increasingly important tool in analytical chemistry, biosciences, and medicine. Heterogeneous assays commonly utilize magnetic ... ...

    Abstract Droplet-based microfluidic systems offer a high potential for miniaturization and automation. Therefore, they are becoming an increasingly important tool in analytical chemistry, biosciences, and medicine. Heterogeneous assays commonly utilize magnetic beads as a solid phase. However, the sensitivity of state of the art microfluidic systems is limited by the high bead concentrations required for efficient extraction across the water–oil interface. Furthermore, current systems suffer from a lack of technical solutions for sequential measurements of multiple samples, limiting their throughput and capacity for automation. Taking advantage of the different wetting properties of hydrophilic and hydrophobic areas in the channels, we improve the extraction efficiency of magnetic beads from aqueous nanoliter-sized droplets by 2 orders of magnitude to the low μg/mL range. Furthermore, the introduction of a switchable magnetic trap enables repetitive capture and release of magnetic particles for sequential analysis of multiple samples, enhancing the throughput. In comparison to conventional ELISA-based sandwich immunoassays on microtiter plates, our microfluidic setup offers a 25–50-fold reduction of sample and reagent consumption with up to 50 technical replicates per sample. The enhanced sensitivity and throughput of this system open avenues for the development of automated detection of biomolecules at the nanoliter scale.
    Keywords analytical chemistry ; automation ; biochemical compounds ; enzyme-linked immunosorbent assay ; hydrophilicity ; hydrophobicity ; magnetism ; medicine ; oil-water interface
    Language English
    Dates of publication 2020-0605
    Size p. 10283-10290.
    Publishing place American Chemical Society
    Document type Article
    Note NAL-AP-2-clean
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.0c00187
    Database NAL-Catalogue (AGRICOLA)

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  4. Article ; Online: Breaking the Interface: Efficient Extraction of Magnetic Beads from Nanoliter Droplets for Automated Sequential Immunoassays.

    Metzler, Lukas / Rehbein, Ulrike / Schönberg, Jan-Niklas / Brandstetter, Thomas / Thedieck, Kathrin / Rühe, Jürgen

    Analytical chemistry

    2020  Volume 92, Issue 15, Page(s) 10283–10290

    Abstract: Droplet-based microfluidic systems offer a high potential for miniaturization and automation. Therefore, they are becoming an increasingly important tool in analytical chemistry, biosciences, and medicine. Heterogeneous assays commonly utilize magnetic ... ...

    Abstract Droplet-based microfluidic systems offer a high potential for miniaturization and automation. Therefore, they are becoming an increasingly important tool in analytical chemistry, biosciences, and medicine. Heterogeneous assays commonly utilize magnetic beads as a solid phase. However, the sensitivity of state of the art microfluidic systems is limited by the high bead concentrations required for efficient extraction across the water-oil interface. Furthermore, current systems suffer from a lack of technical solutions for sequential measurements of multiple samples, limiting their throughput and capacity for automation. Taking advantage of the different wetting properties of hydrophilic and hydrophobic areas in the channels, we improve the extraction efficiency of magnetic beads from aqueous nanoliter-sized droplets by 2 orders of magnitude to the low μg/mL range. Furthermore, the introduction of a switchable magnetic trap enables repetitive capture and release of magnetic particles for sequential analysis of multiple samples, enhancing the throughput. In comparison to conventional ELISA-based sandwich immunoassays on microtiter plates, our microfluidic setup offers a 25-50-fold reduction of sample and reagent consumption with up to 50 technical replicates per sample. The enhanced sensitivity and throughput of this system open avenues for the development of automated detection of biomolecules at the nanoliter scale.
    MeSH term(s) Antibodies/chemistry ; Automation/methods ; Enzyme-Linked Immunosorbent Assay/methods ; Fluorocarbons/chemistry ; Immunomagnetic Separation/methods ; Magnetic Phenomena ; Microfluidic Analytical Techniques/methods ; Nanostructures
    Chemical Substances Antibodies ; Fluorocarbons
    Language English
    Publishing date 2020-06-25
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.0c00187
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4033: 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)

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  5. Article: The TSC Complex-mTORC1 Axis: From Lysosomes to Stress Granules and Back.

    Rehbein, Ulrike / Prentzell, Mirja Tamara / Cadena Sandoval, Marti / Heberle, Alexander Martin / Henske, Elizabeth P / Opitz, Christiane A / Thedieck, Kathrin

    Frontiers in cell and developmental biology

    2021  Volume 9, Page(s) 751892

    Abstract: The tuberous sclerosis protein complex (TSC complex) is a key integrator of metabolic signals and cellular stress. In response to nutrient shortage and stresses, the TSC complex inhibits the mechanistic target of rapamycin complex 1 (mTORC1) at the ... ...

    Abstract The tuberous sclerosis protein complex (TSC complex) is a key integrator of metabolic signals and cellular stress. In response to nutrient shortage and stresses, the TSC complex inhibits the mechanistic target of rapamycin complex 1 (mTORC1) at the lysosomes. mTORC1 is also inhibited by stress granules (SGs), RNA-protein assemblies that dissociate mTORC1. The mechanisms of lysosome and SG recruitment of mTORC1 are well studied. In contrast, molecular details on lysosomal recruitment of the TSC complex have emerged only recently. The TSC complex subunit 1 (TSC1) binds lysosomes
    Language English
    Publishing date 2021-10-29
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2021.751892
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  6. Article ; Online: mTORC1 Crosstalk With Stress Granules in Aging and Age-Related Diseases.

    Cadena Sandoval, Marti / Heberle, Alexander Martin / Rehbein, Ulrike / Barile, Cecilia / Ramos Pittol, José Miguel / Thedieck, Kathrin

    Frontiers in aging

    2021  Volume 2, Page(s) 761333

    Abstract: The mechanistic target of rapamycin complex 1 (mTORC1) kinase is a master regulator of metabolism and aging. A complex signaling network converges on mTORC1 and integrates growth factor, nutrient and stress signals. Aging is a dynamic process ... ...

    Abstract The mechanistic target of rapamycin complex 1 (mTORC1) kinase is a master regulator of metabolism and aging. A complex signaling network converges on mTORC1 and integrates growth factor, nutrient and stress signals. Aging is a dynamic process characterized by declining cellular survival, renewal, and fertility. Stressors elicited by aging hallmarks such as mitochondrial malfunction, loss of proteostasis, genomic instability and telomere shortening impinge on mTORC1 thereby contributing to age-related processes. Stress granules (SGs) constitute a cytoplasmic non-membranous compartment formed by RNA-protein aggregates, which control RNA metabolism, signaling, and survival under stress. Increasing evidence reveals complex crosstalk between the mTORC1 network and SGs. In this review, we cover stressors elicited by aging hallmarks that impinge on mTORC1 and SGs. We discuss their interplay, and we highlight possible links in the context of aging and age-related diseases.
    Language English
    Publishing date 2021-10-13
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 3076785-4
    ISSN 2673-6217 ; 2673-6217
    ISSN (online) 2673-6217
    ISSN 2673-6217
    DOI 10.3389/fragi.2021.761333
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. 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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    Zs.A 1167: Show issues Location:
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