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pro vyhledávání: '"Shon Cohen"'
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
Autor:
Shon Cohen, Dina Schneidman‐Duhovny
Publikováno v:
PROTEOMICS.
Publikováno v:
Journal of Proteome Research. 20:3701-3708
Cross-linking of living cells followed by mass spectrometry identification of cross-linked peptides (in situ CLMS) is an emerging technology to study protein structures in their native environment. One of the inherent difficulties of this technology
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