Zobrazeno 1 - 10
of 12
pro vyhledávání: '"D. Alex Crowder"'
Autor:
Frantisek Filandr, Vladimir Sarpe, Shaunak Raval, D. Alex Crowder, Morgan F. Khan, Pauline Douglas, Stephen Coales, Rosa Viner, Aleem Syed, John A. Tainer, Susan P. Lees-Miller, David C. Schriemer
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-12 (2024)
Abstract We present a hydrogen/deuterium exchange workflow coupled to tandem mass spectrometry (HX-MS2) that supports the acquisition of peptide fragment ions alongside their peptide precursors. The approach enables true auto-curation of HX data by m
Externí odkaz:
https://doaj.org/article/8c900839ad1c4b10a419586ee7d79785
Autor:
Frantisek Filandr, Vladimir Sarpe, Shaunak Raval, D. Alex Crowder, Morgan F. Khan, Pauline Douglas, Stephen Coales, Rosa Viner, Aleem Syed, John A. Tainer, Susan P. Lees-Miller, David C. Schriemer
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-1 (2024)
Externí odkaz:
https://doaj.org/article/165f5b3a8f494e12ab6cbfdea6535412
Autor:
Atefeh Rafiei, Sofía Cruz Tetlalmatzi, Claire H Edrington, Linda Lee, D Alex Crowder, Daniel J Saltzberg, Andrej Sali, Gary Brouhard, David C Schriemer
Publikováno v:
eLife, Vol 11 (2022)
Doublecortin (DCX) is a microtubule (MT)-associated protein that regulates MT structure and function during neuronal development and mutations in DCX lead to a spectrum of neurological disorders. The structural properties of MT-bound DCX that explain
Externí odkaz:
https://doaj.org/article/c0c1f63c70ab443d8a4198aa65ca6e7b
Autor:
D. Alex Crowder, Vladimir Sarpe, Bruno C. Amaral, Nicholas I. Brodie, Andrew R. M. Michael, David Schriemer
Crosslinking mass spectrometry (XL-MS) is a valuable technique for the generation of point-to-point distance measurements in protein space. Applications involvingin situchemical crosslinking have created the possibility of mapping whole protein inter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0d15943aee838afd645b17fe4b5b8235
https://doi.org/10.1101/2023.01.20.524983
https://doi.org/10.1101/2023.01.20.524983
Autor:
Rosa Viner, Vladimir Sarpe, David C. Schriemer, Morgan Hepburn, Terry Zhang, Shaunak Raval, D. Alex Crowder
Publikováno v:
Analytical Chemistry. 93:4246-4254
The data analysis practices associated with hydrogen-deuterium exchange mass spectrometry (HX-MS) lag far behind that of most other MS-based protein analysis tools. A reliance on external tools from other fields and a persistent need for manual data
Autor:
Atefeh Rafiei, Sofía Cruz Tetlalmatzi, Claire H Edrington, Linda Lee, D Alex Crowder, Daniel J Saltzberg, Andrej Sali, Gary Brouhard, David C Schriemer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4cce8fffffa962b2181db1c13c8685f1
https://doi.org/10.7554/elife.66975.sa2
https://doi.org/10.7554/elife.66975.sa2
Autor:
Daniel S. Ziemianowicz, Daniel J. Saltzberg, D. Alex Crowder, Christoph U. Schräder, Andrej Sali, Troy J. Pells, Morgan Hepburn, David C. Schriemer
Publikováno v:
Molecular & Cellular Proteomics : MCP
Proteomics methodology has expanded to include protein structural analysis, primarily through cross-linking mass spectrometry (XL-MS) and hydrogen–deuterium exchange mass spectrometry (HX-MS). However, while the structural proteomics community has
Autor:
Linda Lee, D. Alex Crowder, Andrej Sali, Daniel J. Saltzberg, Atefeh Rafiei, Gary J. Brouhard, David C. Schriemer
Doublecortin (DCX) is a microtubule (MT) associated protein that regulates MT structure and function during neuronal development and mutations in DCX lead to a spectrum of neurological disorders. The structural properties of MT-bound DCX remain poorl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d933529675ddf82c93d28bb21a6cc664
https://doi.org/10.1101/2021.02.17.431714
https://doi.org/10.1101/2021.02.17.431714
Autor:
Morgan Hepburn, Atefeh Rafiei, David C. Schriemer, Vladimir Sarpe, Troy J. Pells, Shaunak Raval, Daniel S. Ziemianowicz, D. Alex Crowder
Publikováno v:
Journal of Proteomics. 225:103844
Structural Mass Spectrometry (SMS) provides a comprehensive toolbox for the analysis of protein structure and function. It offers multiple sources of structural information that are increasingly useful for integrative structural modeling of complex p