Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Christine Piotrowski"'
Autor:
Christine Piotrowski, Rocco Moretti, Christian H. Ihling, André Haedicke, Thomas Liepold, Noa Lipstein, Jens Meiler, Olaf Jahn, Andrea Sinz
Publikováno v:
Cells, Vol 9, Iss 1, p 136 (2020)
Exploring the interactions between the Ca2+ binding protein calmodulin (CaM) and its target proteins remains a challenging task. Members of the Munc13 protein family play an essential role in short-term synaptic plasticity, modulated via the interact
Externí odkaz:
https://doaj.org/article/e1350fa1e43240d194db6504431ef382
Autor:
Christian Ihling, Andrea Sinz, Noa Lipstein, Jens Meiler, Olaf Jahn, André Haedicke, Christine Piotrowski, Rocco Moretti, Thomas Liepold
Publikováno v:
Cells, Vol 9, Iss 1, p 136 (2020)
Cells
Volume 9
Issue 1
Cells
Volume 9
Issue 1
Exploring the interactions between the Ca2+ binding protein calmodulin (CaM) and its target proteins remains a challenging task. Members of the Munc13 protein family play an essential role in short-term synaptic plasticity, modulated via the interact
Autor:
Christine Piotrowski, Andrea Sinz, Mathias Schäfer, Christian Arlt, Christian Ihling, Christoph Hage, Michael Götze, Rico Schmidt, Claudio Iacobucci
Publikováno v:
Nature Protocols. 13:2864-2889
Chemical cross-linking in combination with mass spectrometric analysis of the created cross-linked products is an emerging technology aimed at deriving valuable structural information from proteins and protein complexes. The goal of our protocol is t
Publikováno v:
Journal of the American Society for Mass Spectrometry. 30:139-148
Cleavable cross-linkers are gaining increasing importance for chemical cross-linking/mass spectrometry (MS) as they permit a reliable and automated data analysis in structural studies of proteins and protein assemblies. Here, we introduce 1,3-diallyl
Autor:
Christine Piotrowski, Christian Arlt, Christian Ihling, Michael Götze, Claudio Iacobucci, Christoph Hage, Anne Rehkamp, Andrea Sinz
Publikováno v:
Analytical Chemistry. 90:2805-2809
A major challenge in cross-linking/mass spectrometry (MS) is targeting carboxyl functions in proteins under physiological conditions that do not disturb the protein's conformation. Cross-linking of glutamic acid and aspartic acid residues in proteins
Publikováno v:
Expert Review of Proteomics. 14:223-242
Introduction: Calmodulin (CaM) is a highly conserved Ca2+-binding protein that is exceptionally abundant in the brain. In the presynaptic compartment of neurons, CaM transduces changes in Ca2+ concentration into the regulation of synaptic transmissio
Autor:
Christine, Piotrowski, Andrea, Sinz
Publikováno v:
Advances in experimental medicine and biology. 1105
During the last two decades, cross-linking combined with mass spectrometry (MS) has evolved as a valuable tool to gain structural insights into proteins and protein assemblies. Structural information is obtained by introducing covalent connections be
Autor:
Michael R. Hoopmann, Nufar Edinger, Caroline Haupt, Solis-Mezarino, Michael Götze, Yufei Xiang, Ravit Mesika, Michael J. MacCoss, Ninnis R, Juri Rappsilber, Huang L, Christoph H. Borchers, Heck Ajr, Chris P. Sarnowski, Daniel S. Ziemianowicz, Nesati, Alex Zelter, Francis J. O’Reilly, Cecilia Emanuelsson, Ruedi Aebersold, Gianluca Degliesposti, Christine Piotrowski, Heike Stephanowitz, Alexander Leitner, Nicholas I. Brodie, Dana Reichmann, Nagarjuna Nagaraj, Carolin Sailer, Kasper D. Rand, Karl Mechtler, Fabio C. Gozzo, Amaral Bc, Carla Schmidt, Gutierrez C, Oleg Klykov, Franz Herzog, Manolo Plasencia, Petr Novák, Stéphane Claverol, Florian Stengel, Richard A. Scheltema, Meng-Qiu Dong, Christian E. Stieger, Matthias Pelzing, David C. Schriemer, Juan D. Chavez, Andrea Sinz, Fan Liu, Nir Kalisman, Şule Yılmaz, Jürgen Cox, Yi Shi, Stéphane Chaignepain, Philip C. Andrews, Zdeněk Kukačka, Frank Sobott, Moriya Slavin, Robert L. Moritz, Lolita Piersimoni, Evgeniy V. Petrotchenko, James E. Bruce, Tara L. Pukala, Michael J. Trnka, J. M. Skehel, Claudio Iacobucci, Rosa Viner, Marta Vilaseca
The number of publications in the field of chemical cross-linking combined with mass spectrometry (XL-MS) to derive constraints for protein three-dimensional structure modeling and to probe protein-protein interactions has largely increased during th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39734b91a442fd5fc7e0ef0b4292d8ba
https://doi.org/10.1101/424697
https://doi.org/10.1101/424697
Autor:
Andrea Sinz, Christine Piotrowski
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9789811321993
During the last two decades, cross-linking combined with mass spectrometry (MS) has evolved as a valuable tool to gain structural insights into proteins and protein assemblies. Structural information is obtained by introducing covalent connections be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::64a74427c3dcab943f6e84987dbbb83e
https://doi.org/10.1007/978-981-13-2200-6_8
https://doi.org/10.1007/978-981-13-2200-6_8
Publikováno v:
Methods (San Diego, Calif.). 89
Photo-induced cross-linking is a highly promising technique to investigate protein conformations and protein-protein interactions in their natural cellular environment. One strategy relies on the non-directed incorporation of diazirine-containing pho