Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Moriya Slavin"'
Autor:
Clothilde Claus, Moriya Slavin, Eugénie Ansseau, Céline Lancelot, Karimatou Bah, Saskia Lassche, Manon Fiévet, Anna Greco, Sara Tomaiuolo, Alexandra Tassin, Virginie Dudome, Benno Kusters, Anne-Emilie Declèves, Dalila Laoudj-Chenivesse, Baziel G. M. van Engelen, Denis Nonclercq, Alexandra Belayew, Nir Kalisman, Frédérique Coppée
Publikováno v:
Skeletal Muscle, Vol 13, Iss 1, Pp 1-30 (2023)
Abstract Background We have previously demonstrated that double homeobox 4 centromeric (DUX4C) encoded for a functional DUX4c protein upregulated in dystrophic skeletal muscles. Based on gain- and loss-of-function studies we have proposed DUX4c invol
Externí odkaz:
https://doaj.org/article/b5d8d28f164f438eaa5c5e0fc91b58bf
Autor:
Tamar Tayri-Wilk, Moriya Slavin, Joanna Zamel, Ayelet Blass, Shon Cohen, Alex Motzik, Xue Sun, Deborah E. Shalev, Oren Ram, Nir Kalisman
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Formaldehyde (FA) is a popular cross-linking reagent, but applying it for cross-linking mass spectrometry (XLMS) has been largely unsuccessful. Here, the authors show that cross-links in structured proteins are the product of two FA molecules and ide
Externí odkaz:
https://doaj.org/article/241e25d8cf7443558ebf3920295f87b0
Publikováno v:
Analytical Chemistry
Development of new reagents for protein cross-linking is constantly ongoing. The chemical formulas for the linker adducts formed by these reagents are usually deduced from expert knowledge and then validated by mass spectrometry. Clearly, it would be
Autor:
Joanna Zamel, Dina Schneidman-Duhovny, Nir Kalisman, Leah Baraz, Miri Stolovich-Rain, Dana G. Wolf, M. Braitbard, Alexander Rouvinski, Moriya Slavin, Ahuva Friedman, Michal Linial, Tsiona Eliyahu, Keren Zohar, Esther S. Brielle
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance We present a generic methodology that extracts structural data from living, intact cells for any protein of interest. Application of this methodology to different viral proteins resulted in significant cross-link sets that revealed the c
Autor:
Shulamit Fluss Ben-Uliel, Faten Habrat Zoabi, Moriya Slavin, Hadas Sibony-Benyamini, Nir Kalisman, Nir Qvit
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 11; Pages: 6076
Mitochondria play central roles in maintaining cellular metabolic homeostasis, cell survival and cell death, and generate most of the cell’s energy. Mitochondria maintain their homeostasis by dynamic (fission and fusion) and quality control mechani
Autor:
Alex Motzik, Oren Ram, Moriya Slavin, Joanna Zamel, Tamar Tayri-Wilk, Nir Kalisman, Shon Cohen, Deborah E. Shalev, Xue Sun, Ayelet Blass
Publikováno v:
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Whole-cell cross-linking coupled to mass spectrometry is one of the few tools that can probe protein–protein interactions in intact cells. A very attractive reagent for this purpose is formaldehyde, a small molecule which is known to rapidly penetr
Autor:
Moriya Slavin, Praveen Kumar Allu, Nir Kalisman, Ben E. Black, C. Xu, M. Braitbard, T. Van Eeuwen, Kenji Murakami, Jennine M. Dawicki-McKenna
Publikováno v:
Curr Biol
Summary Centromeric nucleosomes are at the interface of the chromosome and the kinetochore that connects to spindle microtubules in mitosis. The core centromeric nucleosome complex (CCNC) harbors the histone H3 variant, CENP-A, and its binding protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd1f330bfc39dc5081b2f4fd878e4e7b
https://europepmc.org/articles/PMC6702948/
https://europepmc.org/articles/PMC6702948/
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:
Moriya, Slavin, Nir, Kalisman
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1764
Cross-linking and mass spectrometry is used more and more for the structural analysis of large proteins and protein complexes. Although essentially a low-resolution method, it avoids the main drawbacks of established structural techniques. Particular
Autor:
Moriya Slavin, Nir Kalisman
Publikováno v:
Protein Complex Assembly ISBN: 9781493977581
Cross-linking and mass spectrometry is used more and more for the structural analysis of large proteins and protein complexes. Although essentially a low-resolution method, it avoids the main drawbacks of established structural techniques. Particular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::93f957ba5dd849be1ef95ebe5c3fcb39
https://doi.org/10.1007/978-1-4939-7759-8_11
https://doi.org/10.1007/978-1-4939-7759-8_11