Zobrazeno 1 - 10
of 222
pro vyhledávání: '"Carl Frieden"'
Autor:
Roger D. Klein, Qin Shu, Zachary T. Cusumano, Kanna Nagamatsu, Nathaniel C. Gualberto, Aaron J. L. Lynch, Chao Wu, Wenjie Wang, Neha Jain, Jerome S. Pinkner, Gaya K. Amarasinghe, Scott J. Hultgren, Carl Frieden, Matthew R. Chapman
Publikováno v:
mBio, Vol 9, Iss 4 (2018)
ABSTRACT Curli amyloid fibers are produced as part of the extracellular biofilm matrix and are composed primarily of the major structural subunit CsgA. The CsgE chaperone facilitates the secretion of CsgA through CsgG by forming a cap at the base of
Externí odkaz:
https://doaj.org/article/ff37b00ca12f43a9a3727996214c28c6
Autor:
Melissa D. Stuchell-Brereton, Maxwell I. Zimmerman, Justin J. Miller, Upasana L. Mallimadugula, J. Jeremías Incicco, Debjit Roy, Louis G. Smith, Jasmine Cubuk, Berevan Baban, Gregory T. DeKoster, Carl Frieden, Gregory R. Bowman, Andrea Soranno
Publikováno v:
Proceedings of the National Academy of Sciences. 120
The ε4-allele variant of apolipoprotein E (ApoE4) is the strongest genetic risk factor for Alzheimer’s disease, although it only differs from its neutral counterpart ApoE3 by a single amino acid substitution. While ApoE4 influences the formation o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::982d41c6d061a85d64b3f74b0017d55a
https://doi.org/10.1073/pnas.2215371120
https://doi.org/10.1073/pnas.2215371120
Autor:
Carl Frieden, Robert Flaumenhaft, Tomasz Heyduk, Nicola Pozzi, Mathivanan Chinnaraj, David A. Barrios
Publikováno v:
Chembiochem
Folding of newly synthesized proteins in the endoplasmic reticulum is assisted by several families of enzymes. One such family is the protein disulfide isomerases (PDIs). PDIs are oxidoreductases, capable of forming new disulfide bonds or breaking ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6afda39b2b3d1597724f3628e12e0cd1
https://doi.org/10.1002/cbic.202000537
https://doi.org/10.1002/cbic.202000537
Autor:
Carl Frieden, Eliza A. Ruben, Prafull S. Gandhi, Zhiwei Chen, Sarah K. Koester, Gregory T. DeKoster, Enrico Di Cera
Publikováno v:
The Journal of Biological Chemistry
The conformational properties of trypsin-like proteases and their zymogen forms remain controversial because of a lack of sufficient information on their free forms. Specifically, it is unclear whether the free protease is zymogen-like and shifts to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d050288428b8d46a9793fca5abe6b101
https://doi.org/10.1074/jbc.ra120.013419
https://doi.org/10.1074/jbc.ra120.013419
Autor:
Carl Frieden, Farha Khan, Gregory T. DeKoster, John T. Petroff, Lawrence J. Chen, Jeff Abramson, Wayland W.L. Cheng, Ailing Tong
Publikováno v:
Anal Chem
Native mass spectrometry paired with ion mobility (IM-MS) provides the capacity to monitor the structure of protein complexes and simultaneously assess small molecule binding to the protein. Native IM-MS typically utilizes positive mode electrospray
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::492637df9035708ba456726166914924
https://doi.org/10.1021/acs.analchem.0c00454
https://doi.org/10.1021/acs.analchem.0c00454
Autor:
Melissa D. Stuchell-Brereton, Maxwell I. Zimmerman, Justin J. Miller, Upasana L. Mallimadugula, J. Jeremias Incicco, Debjit Roy, Louis G. Smith, Berevan Baban, Gregory T. DeKoster, Carl Frieden, Gregory R. Bowman, Andrea Soranno
The ε4-allele variant of Apolipoprotein E (ApoE4) is the strongest genetic risk factor for Alzheimer’s disease, though it only differs from its neutral counterpart ApoE3 by a single amino acid substitution. While ApoE4 influences the formation of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7150579344a81feb2ed19d91697f30c4
https://doi.org/10.1101/2022.02.02.478828
https://doi.org/10.1101/2022.02.02.478828
Autor:
Melissa D. Stuchell-Brereton, Maxwell I. Zimmerman, Justin J. Miller, Upasana L. Mallimadugula, Juan J. Incicco, Debjit Roy, Louis G. Smith, Jasmine Cubuk, Berevan Baban, Gregory T. DeKoster, Carl Frieden, Gregory R. Bowman, Andrea Soranno
Publikováno v:
Biophysical Journal. 122:329a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e2cd2c4d2c7261e4aab52d66d8e37a8a
https://doi.org/10.1016/j.bpj.2022.11.1840
https://doi.org/10.1016/j.bpj.2022.11.1840
Autor:
Hu Wang, Bradley F. Boeve, Michael G. Heckman, Yingxue Ren, Yan W. Asmann, Ana-Caroline Raulin, Yuan Fu, Thomas R. Caulfield, Tadafumi C. Ikezu, Tanis J. Ferman, Cynthia Linares, Lin Jia, Dennis W. Dickson, Carl Frieden, Jing Zhao, Owen A. Ross, Steven G. Younkin, Zbigniew K. Wszolek, Val J. Lowe, Cassandra L. Rosenberg, David S. Knopman, Xia Li, Yonghe Li, John D. Fryer, Xue Wang, Sydney V. Doss, Melissa E. Murray, Wenyan Lu, Clifford R. Jack, Melissa C. Wren, Xianlin Han, Joshua Knight, Zachary A. Trottier, Na Wang, Yuka A. Martens, Joseph E. Parisi, Yixing Chen, Guojun Bu, Aishe Kurti, Neill R. Graff-Radford, Kejal Kantarci, Chia Chen Liu, Glenn E. Smith, Ronald C. Petersen, Prashanthi Vemuri, Na Zhao, Francis Shue
Publikováno v:
BASE-Bielefeld Academic Search Engine
A rare APOE variant APOE3 -Jac reduces self-aggregation and promotes healthy brain aging.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bf0cad4b9e597fca676ddff7a6faa0a
https://doi.org/10.1126/scitranslmed.abc9375
https://doi.org/10.1126/scitranslmed.abc9375
Autor:
Melissa D. Stuchell-Brereton, Maxwell I. Zimmerman, Upasana L. Mallimadugula, J. Jeremias Incicco, Debjit Roy, Berevan Baban, Gregory T. DeKoster, Gregory Bowman, Carl Frieden, Andrea Soranno
Publikováno v:
Biophysical Journal. 121:182a-183a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6030addd3abebac20d78830b9fbfd856
https://doi.org/10.1016/j.bpj.2021.11.1841
https://doi.org/10.1016/j.bpj.2021.11.1841
Autor:
Carl Frieden
Publikováno v:
Protein Science. 28:837-842
It has been estimated that 30%-50% of proteins self-assemble to form complexes consisting of multiple copies of themselves. If there is a functional difference between different molecular weight forms and if these forms interconvert on a reasonable t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::527876dc09405447156188f89e9c16ec
https://doi.org/10.1002/pro.3583
https://doi.org/10.1002/pro.3583