Zobrazeno 1 - 10
of 63
pro vyhledávání: '"M. Lubner"'
Autor:
Zhe Li, Shunzhi Wang, Una Nattermann, Asim K. Bera, Andrew J. Borst, Matthew J. Bick, Erin C. Yang, William Sheffler, Byeongdu Lee, Soenke Seifert, Hannah Nguyen, Alex Kang, Radhika Dalal, Joshua M. Lubner, Yang Hsia, Hugh Haddox, Alexis Courbet, Quinton Dowling, Marcos Miranda, Andrew Favor, Ali Etemadi, Natasha I. Edman, Wei Yang, Banumathi Sankaran, Babak Negahdari, David Baker
SummaryProtein crystallization plays a central role in structural biology1, with broad impact2in pharmaceutical formulation3, drug delivery4, biosensing5, and biocatalysis6,7. Despite this importance, the process of protein crystallization remains po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::97c9e49b9bf954ca7ba67cff48a16384
https://doi.org/10.1101/2022.11.18.517014
https://doi.org/10.1101/2022.11.18.517014
Autor:
J. Winterholler, M. Kisting, K. Falk, A. Kisting, J. White, M. Lubner, P. Laeseke, L. Mankowski-Gettle, L. Stratchko, J. Swietlik, J. Hinshaw, T. Ferreira, T. McCormick, F. Lee, T. Ziemlewicz
Publikováno v:
Journal of Vascular and Interventional Radiology. 34:S156
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4a8a44375fc7efe832eab90d5332e914
https://doi.org/10.1016/j.jvir.2022.12.417
https://doi.org/10.1016/j.jvir.2022.12.417
Autor:
A. Couillard, M. Kisting, A. Rossebo, E. Knott, T. Ziemlewicz, L. Stratchko, M. Lubner, E. Knavel, J. Swietlik, P. Laeseke, J. Abel, F. Lee
Publikováno v:
Journal of Vascular and Interventional Radiology. 33:S25-S26
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e53be55661f5ea09818ef6726afb87f1
https://doi.org/10.1016/j.jvir.2022.03.134
https://doi.org/10.1016/j.jvir.2022.03.134
Autor:
Michael F Chou, Sladjana Prisic, Joshua M Lubner, George M Church, Robert N Husson, Daniel Schwartz
Publikováno v:
PLoS ONE, Vol 7, Iss 12, p e52747 (2012)
The identification of protein kinase targets remains a significant bottleneck for our understanding of signal transduction in normal and diseased cellular states. Kinases recognize their substrates in part through sequence motifs on substrate protein
Externí odkaz:
https://doaj.org/article/74986d65be9f43b0a21e7ec887eb6ebc
Publikováno v:
Computational Biology and Chemistry. 70:107-115
Human peptidylarginine deiminases (hPADs) are a family of five calcium-dependent enzymes that facilitate citrullination, which is the post-translational modification of peptidyl arginine to peptidyl citrulline. The isozymes hPAD2 and hPAD4 have been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cdcc4c6f296fe744c2a5b4edda03d6d3
https://doi.org/10.1016/j.compbiolchem.2017.08.001
https://doi.org/10.1016/j.compbiolchem.2017.08.001
Autor:
Kimberly L. Dodge-Kafka, Joshua M. Lubner, George M. Church, Cathrine R. Carlson, Michael F. Chou, Daniel Schwartz
Publikováno v:
FEBS Letters. 591:459-467
The PKAL205R hotspot mutation has been implicated in Cushing's syndrome through hyperactive gain-of-function PKA signaling; however, its influence on substrate specificity has not been investigated. Here, we employ the Proteomic Peptide Library (ProP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::15d98f9154ed0b4817265d9ce3889773
https://doi.org/10.1002/1873-3468.12562
https://doi.org/10.1002/1873-3468.12562
Autor:
Kimberly L. Dodge-Kafka, Daniel Schwartz, Joshua M. Lubner, George M. Church, Cathrine R. Carlson, Michael F. Chou
The PKAL205R hotspot mutation has been implicated in Cushing’s Syndrome through hyperactive gain-of-function PKA signaling, however its influence on substrate specificity has not been investigated. Here, we employ the Proteomic Peptide Library (Pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c1b5afd99c0641f9a5873e3d60d6606
https://doi.org/10.1101/091231
https://doi.org/10.1101/091231
Protein kinase specificity is largely imparted through substrate binding pocket motifs. Missense mutations in these regions are frequently associated with human disease, and in some cases can alter substrate specificity. However, current efforts at d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1fad1ade9a39e1f8c689551f3c9ad37
https://doi.org/10.1101/091892
https://doi.org/10.1101/091892
Autor:
Joshua M, Lubner, Kimberly L, Dodge-Kafka, Cathrine R, Carlson, George M, Church, Michael F, Chou, Daniel, Schwartz
Publikováno v:
FEBS letters. 591(3)
The PKAL205R hotspot mutation has been implicated in Cushing’s Syndrome through hyperactive gain-of-function PKA signaling, however its influence on substrate specificity has not been investigated. Here, we employ the Proteomic Peptide Library (Pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2a72c02b9c51bb887b8eedc20eaf9c1a
https://pubmed.ncbi.nlm.nih.gov/28100013
https://pubmed.ncbi.nlm.nih.gov/28100013
Publikováno v:
Current Protocols in Chemical Biology. 10:e38
Characterizing protein kinase substrate specificity motifs represents a powerful step in elucidating kinase-signaling cascades. The protocol described here uses a bacterial system to evaluate kinase specificity motifs in vivo, without the need for ra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca4a8170d36fc5c8b30a7b42a4c2bea1
https://doi.org/10.1002/cpch.38
https://doi.org/10.1002/cpch.38