Publications

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1579 Publications visible to you, out of a total of 1579

Abstract

Not specified

Authors: Patrick A. Ondratschek, Friedrich K. Röpke, Fabian R. N. Schneider, Christian Fendt, Christian Sand, Sebastian T. Ohlmann, Rüdiger Pakmor, Volker Springel

Date Published: 1st Apr 2022

Publication Type: Journal

Abstract

Not specified

Authors: Patrick A. Ondratschek, Friedrich K. Röpke, Fabian R. N. Schneider, Christian Fendt, Christian Sand, Sebastian T. Ohlmann, Rüdiger Pakmor, Volker Springel

Date Published: 1st Apr 2022

Publication Type: Journal

Abstract

Not specified

Authors: Richard Miller, Marco Ajello, Katie Auchettl, John Beacom, Peter Bloser, Adam Burrows, Anna Frebel, Chris Fryer, Dieter Hartmann, Peter Hoeflich, Aimee Hungerford, Mark Leising, Laura Lopez, Peter Milne, Patrick Peplowski, Friedrich Roepke, Daniel Scolnic, Ivo Seitenzahl, LihSin The, C. Young

Date Published: 1st Apr 2022

Publication Type: InProceedings

Abstract

Not specified

Authors: Richard Miller, Marco Ajello, Katie Auchettl, John Beacom, Peter Bloser, Adam Burrows, Anna Frebel, Chris Fryer, Dieter Hartmann, Peter Hoeflich, Aimee Hungerford, Mark Leising, Laura Lopez, Peter Milne, Patrick Peplowski, Friedrich Roepke, Daniel Scolnic, Ivo Seitenzahl, Lih-Sin The, C. Alex Young, LOX Team

Date Published: 1st Apr 2022

Publication Type: InProceedings

Abstract (Expand)

Macrophage-1 antigen or Mac-1 (CD11b/CD18, αMβ2) is a leukocyte integrin essential for firm adhesion of neutrophils, lymphocytes and monocytes against flow when recruited to the endothelium. To migrate to the site of inflammation, leukocytes require coordinated adhesion and de-adhesion for directional movement. The vascular thiol isomerase, protein disulfide isomerase (PDI), was found by fluorescence microscopy to colocalize with high affinity Mac-1 at the trailing edge of stimulated neutrophils when adhered to ICAM-1 under fluid shear. From differential cysteine alkylation and mass spectrometry studies, PDI cleaves two allosteric disulfide bonds, C169-C176 and C224-C264, in the βI domain of the β2 subunit, and in mutagenesis and cell transfection studies, cleavage of the C224-C264 disulfide bond was shown to selectively control Mac-1 dis-engagement from ICAM-1 under fluid shear. Molecular dynamics simulations and binding of conformation-specific antibodies reveal that cleavage of the C224-C264 bond induces conformational change and mechanical stress in the βI domain that allosterically alters exposure of an αI domain epitope and shifts Mac-1 to a lower affinity state. From studies of neutrophil adherence to ICAM-1 under fluid shear, these molecular events promote neutrophil motility in the direction of flow at high shear stress. In summary, shear-dependent PDI cleavage of neutrophil Mac-1 C224-C264 disulfide bond triggers Mac-1 de-adherence from ICAM-1 at the trailing edge of the cell and enables directional movement of neutrophils during inflammation.

Authors: Alexander Dupuy, Camilo Aponte-Santamaría, Adva Yeheskel, Frauke Gräter, Philip J. Hogg, Freda H. Passam, Joyce Chiu

Date Published: 30th Mar 2022

Publication Type: Journal

Abstract (Expand)

Focal adhesions link the actomyosin cytoskeleton to the extracellular matrix regulating cell adhesion, shape, and migration. Adhesions are dynamically assembled and disassembled in response to extrinsic and intrinsic forces, but how the essential adhesion component intergrin-linked kinase (ILK) dynamically responds to mechanical force and what role ATP bound to this pseudokinase plays remains elusive. Here, we apply force-probe molecular dynamics simulations of human ILK:α-parvin coupled to traction force microscopy to explore ILK mechanotransducing functions. We identify two key saltbridge-forming arginines within the allosteric, ATP-dependent force-propagation network of ILK. Disrupting this network by mutation impedes parvin binding, focal adhesion stabilization, force generation, and thus migration. Under tension, ATP shifts the balance from rupture of the complex to protein unfolding, indicating that ATP increases the force threshold required for focal adhesion disassembly. Our study proposes a new role of ATP as an obligatory binding partner for structural and mechanical integrity of the pseudokinase ILK, ensuring efficient cellular force generation and migration.

Authors: Isabel Martin, Michele Nava, Sara Wickström, Frauke Gräter

Date Published: 8th Mar 2022

Publication Type: Journal

Abstract (Expand)

Abstract We present time-series photometry of 21 nearby type II Cepheids in the near-infrared J , H , and K s passbands. We use this photometry, together with the Third Gaia Early Data Release parallaxes, K s passbands. We use this photometry, together with the Third Gaia Early Data Release parallaxes, to determine for the first time period–luminosity relations (PLRs) for type II Cepheids from field representatives of these old pulsating stars in the near-infrared regime. We found PLRs to be very narrow for BL Herculis stars, which makes them candidates for precision distance indicators. We then use archival photometry and the most accurate distance obtained from eclipsing binaries to recalibrate PLRs for type II Cepheids in the Large Magellanic Cloud (LMC). Slopes of our PLRs in the Milky Way and in the LMC differ by slightly more than 2 σ and are in a good agreement with previous studies of the LMC, Galactic bulge, and Galactic globular cluster type II Cepheids samples. We use PLRs of Milky Way type II Cepheids to measure the distance to the LMC, and we obtain a distance modulus of 18.540 ± 0.026(stat.) ± 0.034(syst.) mag in the W JK Wesenheit index. We also investigate the metallicity effect within our Milky Way sample, and we find a rather significant value of about −0.2 mag dex −1 in each band meaning that more metal-rich type II Cepheids are intrinsically brighter than their more metal-poor counterparts, in agreement with the value obtained from type II Cepheids in Galactic globular clusters. The main source of systematic error on our Milky Way PLRs calibration, and the LMC distance, is the current uncertainty of the Gaia parallax zero-point.

Authors: Piotr Wielgórski, Grzegorz Pietrzyński, Bogumił Pilecki, Wolfgang Gieren, Bartłomiej Zgirski, Marek Górski, Gergely Hajdu, Weronika Narloch, Paulina Karczmarek, Radosław Smolec, Pierre Kervella, Jesper Storm, Alexandre Gallenne, Louise Breuval, Megan Lewis, Mikołaj Kałuszyński, Dariusz Graczyk, Wojciech Pych, Ksenia Suchomska, Mónica Taormina, Gonzalo Rojas Garcia, Aleksandra Kotek, Rolf Chini, Francisco Pozo Nũnez, Sadegh Noroozi, Catalina Sobrino Figaredo, Martin Haas, Klaus Hodapp, Przemysław Mikołajczyk, Krzysztof Kotysz, Dawid Moździerski, Piotr Kołaczek-Szymański

Date Published: 8th Mar 2022

Publication Type: Journal

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