Zobrazeno 1 - 10
of 187
pro vyhledávání: '"P Andrew, Karplus"'
Publikováno v:
Microbiology Spectrum, Vol 11, Iss 6 (2023)
ABSTRACT Polymorphic membrane proteins (Pmps) are chlamydial cell surface proteins with signature repeating FxxN and GGA (I, V, L) tetrapeptide motifs. These autotransporter proteins are key immune targets and mediators of host-microbe interactions b
Externí odkaz:
https://doaj.org/article/17e17e65584a47e29e9714cf0d5f357a
Autor:
Elise M. Van Fossen, Sonia Grutzius, Carl E. Ruby, Dan V. Mourich, Chris Cebra, Shay Bracha, P. Andrew Karplus, Richard B. Cooley, Ryan A. Mehl
Publikováno v:
Frontiers in Chemistry, Vol 10 (2022)
A critical step in developing therapeutics for oxidative stress-related pathologies is the ability to determine which specific modified protein species are innocuous by-products of pathology and which are causative agents. To achieve this goal, techn
Externí odkaz:
https://doaj.org/article/e7ee875dac2c4ee68361d8663535c867
Autor:
Phillip Zhu, Stanislau Stanisheuski, Rachel Franklin, Amber Vogel, Cat Hoang Vesely, Patrick Reardon, Nikolai N. Sluchanko, Joseph S. Beckman, P. Andrew Karplus, Ryan A. Mehl, Richard B. Cooley
Publikováno v:
ACS Central Science. 9:816-835
Publikováno v:
Cell Chemical Biology. 30:343-361
Autor:
Thomas Evangelidis, Santrupti Nerli, Jiří Nováček, Andrew E. Brereton, P. Andrew Karplus, Rochelle R. Dotas, Vincenzo Venditti, Nikolaos G. Sgourakis, Konstantinos Tripsianes
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
Further automation of NMR structure determination is needed to increase the throughput and accessibility of this method. Here the authors present 4D-CHAINS/autoNOE-Rosetta, a complete pipeline that allows rapid and fully automated structure determina
Externí odkaz:
https://doaj.org/article/da44ac29a8c6451eba4c6afcde1322d3
Publikováno v:
ACS Chemical Biology. 17:3470-3477
Autor:
Savanna Avila-Crump, Marcus L. Hemshorn, Chloe M. Jones, Lea Mbengi, Kyle Meyer, Joshua A. Griffis, Subhashis Jana, Grace E. Petrina, Vinayak V. Pagar, P. Andrew Karplus, E. James Petersson, John J. Perona, Ryan A. Mehl, Richard B. Cooley
Publikováno v:
ACS Chemical Biology. 17:3458-3469
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-9 (2017)
Kinesin-14s are commonly considered to be minus end-directed microtubule motor proteins. Here the authors show that KlpA, a fungal kinesin-14 orthologue, relies on its N-terminal nonmotor microtubule-binding tail to achieve context-dependent bidirect
Externí odkaz:
https://doaj.org/article/452fe2c9c270404e86830743dc6002c8
Autor:
Savanna, Avila-Crump, Marcus L, Hemshorn, Chloe M, Jones, Lea, Mbengi, Kyle, Meyer, Joshua A, Griffis, Subhashis, Jana, Grace E, Petrina, Vinayak V, Pagar, P Andrew, Karplus, E James, Petersson, John J, Perona, Ryan A, Mehl, Richard B, Cooley
Publikováno v:
ACS chemical biology. 17(12)
Genetic code expansion (GCE) technologies commonly use the pyrrolysyl-tRNA synthetase (PylRS)/tRNA
Publikováno v:
ACS chemical biology.
A recently developed genetic code expansion (GCE) platform based on the pyrrolysine amino-acyl tRNA synthetase (PylRS)/tRNA