Real-time dynamic single-molecule protein sequencing on an integrated semiconductor device

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6d3367086ac787e208c4c79a68cbb83f
https://doi.org/10.1126/science.abo7651

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Structure-function analysis of Sua5 protein reveals novel functional motifs required for the biosynthesis of the universal t

Autor: Adeline, Pichard-Kostuch, Wenhua, Zhang, Dominique, Liger, Marie-Claire, Daugeron, Juliette, Létoquart, Ines, Li de la Sierra-Gallay, Patrick, Forterre, Bruno, Collinet, Herman, van Tilbeurgh, Tamara, Basta

Publikováno v: RNA (New York, N.Y.). 24(7)

N(6)-threonyl-carbamoyl adenosine (t(6)A) is a universal tRNA modification found at position 37, next to the anticodon, in almost all tRNAs decoding ANN codons (where N = A, U, G, or C). t(6)A stabilizes the codon–anticodon interaction and hence pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::fb7feb078f5c09269184922673e5bce5
https://pubmed.ncbi.nlm.nih.gov/29650678

Function and Biosynthesis of the Universal tRNA Modification N6-Threonylcarbamoyl-Adenosine

Autor: Patrick Forterre, M.C. Daugeron, A. Pichard-Kostuch, Tamara Basta

Publikováno v: RNA Metabolism and Gene Expression in Archaea ISBN: 9783319657943

Transfer RNAs (tRNAs) are essential components of the translation machinery that reads the genetic message and translates it into polypeptides. Apart from the four canonical nucleotides A, C, U and G, tRNAs contain a variety of modified nucleosides w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6458c5e77711d8456266be3e090ea67a
https://doi.org/10.1007/978-3-319-65795-0_8