Zobrazeno 1 - 10
of 38
pro vyhledávání: '"Michael T. Taylor"'
Autor:
Caleb R. Hoopes, Francisco J. Garcia, Akash M. Sarkar, Nicholas J. Kuehl, David T. Barkan, Nicole L. Collins, Glenna E. Meister, Taylor R. Bramhall, Chien-Hsiang Hsu, Michael D. Jones, Markus Schirle, Michael T. Taylor
Publikováno v:
J Am Chem Soc
Tryptophan (Trp) plays a variety of critical functional roles in protein biochemistry however, owing to its low natural frequency and poor nucleophilicity, the design of effective methods for both single protein bioconjugation at Trp as well as for i
Autor:
Michael D. Jones, Francisco J. Garcia, David T. Barkan, Nicole Collins, Chien-Hsang Hsu, Caleb Hoopes, Nicholas J. Kuehl, Michael T. Taylor, Markus Schirle, Akash Sarkar
Tryptophan (Trp) plays a variety of critical functional roles in protein biochemistry however, owing to its low natural frequency and poor nucleophilicity, the design of effective methods for both single protein bioconjugation at Trp as well as for i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d3a52a2cdc1f4ca70f722fd88e0750c
https://doi.org/10.33774/chemrxiv-2021-r2nd2
https://doi.org/10.33774/chemrxiv-2021-r2nd2
Autor:
Oshini Ekanayake, Christopher W. am Ende, Samuel L. Scinto, Uthpala Seneviratne, Samantha J. Boyd, Michael T. Taylor, Sharon Rozovsky, Jessica E. Pigga, Jun Liu, Joseph M. Fox
Publikováno v:
Journal of the American Chemical Society. 141:10932-10937
Sulfenylation (RSH → RSOH) is a post-translational protein modification associated with cellular mechanisms for signal transduction and the regulation of reactive oxygen species. Protein sulfenic acids are challenging to identify and study due to t
Publikováno v:
Synlett
The chemical modification of tryptophan (Trp) has been the subject of interest for nearly 100 years, yet the development of modification conditions that exploit the inherent photolability of Trp has remained elusive. With this perspective, we discuss
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54c89db74b3199e58a76c127c5788ccc
https://europepmc.org/articles/PMC8372833/
https://europepmc.org/articles/PMC8372833/
Publikováno v:
J Am Chem Soc
We report here a photochemical process for the selective modification of tryptophan (Trp) residues in peptides and small proteins using electron-responsive N-carbamoylpyridinium salts and UV-B light. Preliminary mechanistic experiments suggest that t
Publikováno v:
UPCommons. Portal del coneixement obert de la UPC
Universitat Politècnica de Catalunya (UPC)
Universitat Politècnica de Catalunya (UPC)
This APS-prepared version is available for the author(s)’ and/or the employer’s use for educational or research purposes. In this paper we analyze the limits of optical time transfer through atmospheric turbulence and relate those predictions to
Publikováno v:
The Precise Time and Time Interval Systems and Applications Meeting.
Future global clock networks will require time and frequency transfer links capable of spanning intercontinental distances and supporting the stability of state-of-the-art frequency standards. Improved Two-Way Satellite Time and Frequency Transfer (T
Autor:
Samuel L, Scinto, Oshini, Ekanayake, Uthpala, Seneviratne, Jessica E, Pigga, Samantha J, Boyd, Michael T, Taylor, Jun, Liu, Christopher W, Am Ende, Sharon, Rozovsky, Joseph M, Fox
Publikováno v:
J Am Chem Soc
Sulfenylation (RSH ->RSOH) is a posttranslational protein modification associated with cellular mechanisms for signal transduction and the regulation of reactive oxygen species. Protein sulfenic acids are challenging to identify and study due to thei
Autor:
Michael T. Taylor, Meera Radhakrishnan, Shi Tuck, Sasha Maldonado, Simone D'Amico, Jake Hillard, Orien Zeng, Michal Adamkiewicz, Sandip Roy, Anjali Roychowdhury
Publikováno v:
2019 IEEE Aerospace Conference.
The Satellites Team of the Stanford Student Space Initiative (SSI) has designed and built Polar-Orbiting Infrared Tracking Receiver (POINTR), a 1U cubesat payload to demonstrate optical-communications technology. Because of the narrow beam divergence
Nature has a remarkable ability to carry out site-selective post-translational modification of proteins, therefore enabling a marked increase in their functional diversity1. Inspired by this, chemical tools have been developed for the synthetic manip
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89aa1175c587dcbd3262f712164b3ee9
https://www.repository.cam.ac.uk/handle/1810/290467
https://www.repository.cam.ac.uk/handle/1810/290467