Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Douglas H. Pike"'
Autor:
Brian D. Reed, Michael J. Meyer, Valentin Abramzon, Omer Ad, Pat Adcock, Faisal R. Ahmad, Gün Alppay, James A. Ball, James Beach, Dominique Belhachemi, Anthony Bellofiore, Michael Bellos, Juan Felipe Beltrán, Andrew Betts, Mohammad Wadud Bhuiya, Kristin Blacklock, Robert Boer, David Boisvert, Norman D. Brault, Aaron Buxbaum, Steve Caprio, Changhoon Choi, Thomas D. Christian, Robert Clancy, Joseph Clark, Thomas Connolly, Kathren Fink Croce, Richard Cullen, Mel Davey, Jack Davidson, Mohamed M. Elshenawy, Michael Ferrigno, Daniel Frier, Saketh Gudipati, Stephanie Hamill, Zhaoyu He, Sharath Hosali, Haidong Huang, Le Huang, Ali Kabiri, Gennadiy Kriger, Brittany Lathrop, An Li, Peter Lim, Stephen Liu, Feixiang Luo, Caixia Lv, Xiaoxiao Ma, Evan McCormack, Michele Millham, Roger Nani, Manjula Pandey, John Parillo, Gayatri Patel, Douglas H. Pike, Kyle Preston, Adeline Pichard-Kostuch, Kyle Rearick, Todd Rearick, Marco Ribezzi-Crivellari, Gerard Schmid, Jonathan Schultz, Xinghua Shi, Badri Singh, Nikita Srivastava, Shannon F. Stewman, TR Thurston, T. R. Thurston, Philip Trioli, Jennifer Tullman, Xin Wang, Yen-Chih Wang, Eric A. G. Webster, Zhizhuo Zhang, Jorge Zuniga, Smita S. Patel, Andrew D. Griffiths, Antoine M. van Oijen, Michael McKenna, Matthew D. Dyer, Jonathan M. Rothberg
Publikováno v:
Science. 378:186-192
Studies of the proteome would benefit greatly from methods to directly sequence and digitally quantify proteins and detect posttranslational modifications with single-molecule sensitivity. Here, we demonstrate single-molecule protein sequencing using
Autor:
Jennifer Timm, Douglas H. Pike, Joshua A. Mancini, Alexei M. Tyryshkin, Saroj Poudel, Jan A. Siess, Paul M. Molinaro, James J. McCann, Kate M. Waldie, Ronald L. Koder, Paul G. Falkowski, Vikas Nanda
The most ancient processes for energy production in the evolution of life involve the reversible oxidation of molecular hydrogen by hydrogenase. Extant hydrogenase enzymes are complex, comprising hundreds of amino acids and multiple cofactors. We des
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::526222fd361adc0f520d778601ea1a96
https://doi.org/10.1101/2022.04.09.487740
https://doi.org/10.1101/2022.04.09.487740
Autor:
Rosalind E. M. Rickaby, Paul G. Falkowski, Saroj Poudel, Douglas H. Pike, Vikas Nanda, Hagai Raanan, Joshua A. Mancini
Publikováno v:
Proc Natl Acad Sci U S A
Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the most abundant enzyme on Earth. However, its catalytic rate per molecule of protein is extremely slow and the binding of the primary substrate, CO2, is competitively displaced by O2. Hen
Autor:
Alexei M. Tyryshkin, Cristian Trncik, James A. Birrell, Bhanu P. Jagilinki, Dror Noy, Vikas Nanda, Stefan Ilic, Barak Akabayov, Douglas H. Pike, Oliver Einsle, Wolfgang Lubitz, Eckhard Bill
Publikováno v:
ACS Synthetic Biology. 9:3400-3407
In vivo expression of metalloproteins requires specific metal trafficking and incorporation machinery inside the cell. Synthetic designed metalloproteins are typically purified without the target metal, which is subsequently introduced through in vit
Publikováno v:
PLoS ONE, Vol 11, Iss 4, p e0153700 (2016)
Recently, catalytic peptides were introduced that mimicked protease activities and showed promising selectivity of products even in organic solvents where protease cannot perform well. However, their catalytic efficiency was extremely low compared to
Externí odkaz:
https://doaj.org/article/826a34a804b946ee99fbfa345b14cf26
Autor:
Michael H. Hecht, Alexei M. Tyryshkin, Douglas H. Pike, Joshua A. Mancini, Vikas Nanda, Michael S. Wang, Saroj Poudel, Liti Haramaty
Publikováno v:
Biotechnology and Applied Biochemistry. 67:574-585
We explore the capacity of the de novo protein, S824, to incorporate a multinuclear iron-sulfur cluster within the core of a single-chain four-helix bundle. This topology has a high intrinsic designability because sequences are constrained largely by
Autor:
Alexei M. Tyryshkin, Joshua A. Mancini, Vikas Nanda, Jennifer Timm, Douglas H. Pike, Paul G. Falkowski, Saroj Poudel
Publikováno v:
Goldschmidt2021 abstracts.
Cofactor binding sites in proteins often are composed of favorable interactions of specific cofactors with the sidechains and/or backbone protein fold motifs. In many cases these motifs contain left-handed conformations which enable tight turns of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::79fc0f3be45acbf682ea0541ba750231
https://doi.org/10.1101/2020.11.17.367490
https://doi.org/10.1101/2020.11.17.367490
Autor:
Joshua A, Mancini, Douglas H, Pike, Alexei M, Tyryshkin, Liti, Haramaty, Michael S, Wang, Saroj, Poudel, Michael, Hecht, Vikas, Nanda
Publikováno v:
Biotechnology and applied biochemistryReferences. 67(4)
We explore the capacity of the de novo protein, S824, to incorporate a multinuclear iron-sulfur cluster within the core of a single-chain four-helix bundle. This topology has a high intrinsic designability because sequences are constrained largely by
Publikováno v:
Proc Natl Acad Sci U S A
Life on Earth is driven by electron transfer reactions catalyzed by a suite of enzymes that comprise the superfamily of oxidoreductases (Enzyme Classification EC1). Most modern oxidoreductases are complex in their structure and chemistry and must hav