Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Mark R. Ambroso"'
Autor:
Alan K. Okada, Kazuki Teranishi, Mark R. Ambroso, Jose Mario Isas, Elena Vazquez-Sarandeses, Joo-Yeun Lee, Arthur Alves Melo, Priyatama Pandey, Daniel Merken, Leona Berndt, Michael Lammers, Oliver Daumke, Karen Chang, Ian S. Haworth, Ralf Langen
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Lysine acetylation regulates the function of soluble proteins in vivo, yet it remains largely unexplored whether lysine acetylation regulates the function of membrane proteins. Here, the authors map lysine acetylation predominantly in membrane-intera
Externí odkaz:
https://doaj.org/article/969a6247f4f548d799fa269799855a27
Autor:
Sinan Arslan, Francisco J. Garcia, Minghao Guo, Matthew W. Kellinger, Semyon Kruglyak, Jake A. LeVieux, Adeline H. Mah, Haosen Wang, Junhua Zhao, Chunhong Zhou, Andrew Altomare, John Bailey, Matthew B. Byrne, Chiting Chang, Steve X. Chen, Byungrae Cho, Claudia N. Dennler, Vivian T. Dien, Derek Fuller, Ryan Kelley, Omid Khandan, Michael G. Klein, Michael Kim, Bryan R. Lajoie, Bill Lin, Yu Liu, Tyler Lopez, Peter T. Mains, Andrew D. Price, Samantha R. Robertson, Hermes Taylor-Weiner, Ramreddy Tippana, Austin B. Tomaney, Su Zhang, Minna Abtahi, Mark R. Ambroso, Rosita Bajari, Ava M. Bellizzi, Chris B. Benitez, Daniel R. Berard, Lorenzo Berti, Kelly N. Blease, Angela P. Blum, Andrew M. Boddicker, Leo Bondar, Chris Brown, Chris A. Bui, Juan Calleja-Aguirre, Kevin Cappa, Joshua Chan, Victor W. Chang, Katherine Charov, Xiyi Chen, Rodger M. Constandse, Weston Damron, Mariam Dawood, Nicole DeBuono, John D. Dimalanta, Laure Edoli, Keerthana Elango, Nikka Faustino, Chao Feng, Matthew Ferrari, Keith Frankie, Adam Fries, Anne Galloway, Vlad Gavrila, Gregory J. Gemmen, James Ghadiali, Arash Ghorbani, Logan A. Goddard, Adriana Roginski Guetter, Garren L. Hendricks, Jendrik Hentschel, Daniel J. Honigfort, Yun-Ting Hsieh, Yu-Hsien Hwang Fu, Scott K. Im, Chaoyi Jin, Shradha Kabu, Daniel E. Kincade, Shawn Levy, Yu Li, Vincent K. Liang, William H. Light, Jonathan B. Lipsher, Tsung-li Liu, Grace Long, Rui Ma, John M. Mailloux, Kyle A. Mandla, Anyssa R. Martinez, Max Mass, Daniel T. McKean, Michael Meron, Edmund A. Miller, Celyne S. Moh, Rachel K. Moore, Juan Moreno, Jordan M. Neysmith, Cassandra S. Niman, Jesus M. Nunez, Micah T. Ojeda, Sara Espinosa Ortiz, Jenna Owens, Geoffrey Piland, Daniel J. Proctor, Josua B. Purba, Michael Ray, Daisong Rong, Virginia M. Saade, Sanchari Saha, Gustav Santo Tomas, Nicholas Scheidler, Luqmanal H. Sirajudeen, Samantha Snow, Gudrun Stengel, Ryan Stinson, Michael J. Stone, Keoni J. Sundseth, Eileen Thai, Connor J. Thompson, Marco Tjioe, Christy L. Trejo, Greg Trieger, Diane Ni Truong, Ben Tse, Benjamin Voiles, Henry Vuong, Jennifer C. Wong, Chiung-Ting Wu, Hua Yu, Yingxian Yu, Ming Yu, Xi Zhang, Da Zhao, Genhua Zheng, Molly He, Michael Previte
Publikováno v:
Nature Biotechnology.
We present avidity sequencing, a sequencing chemistry that separately optimizes the processes of stepping along a DNA template and that of identifying each nucleotide within the template. Nucleotide identification uses multivalent nucleotide ligands
Autor:
Leona Berndt, Elena Vazquez-Sarandeses, Arthur Alves de Melo, Kazuki Teranishi, Ralf Langen, Mark R. Ambroso, Michael Lammers, Daniel Merken, Oliver Daumke, Ian S. Haworth, Joo-Yeun Lee, Alan K Okada, Jose Mario Isas, Karen Chang, Priyatama Pandey
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nature Communications
Nature Communications
Lysine acetylation regulates the function of soluble proteins in vivo, yet it remains largely unexplored whether lysine acetylation regulates membrane protein function. Here, we use bioinformatics, biophysical analysis of recombinant proteins, live-c
Autor:
Sinan Arslan, Francisco J. Garcia, Minghao Guo, Matthew W. Kellinger, Semyon Kruglyak, Jake A. LeVieux, Adeline H. Mah, Haosen Wang, Junhua Zhao, Chunhong Zhou, Andrew Altomare, John Bailey, Matthew B. Byrne, Chiting Chang, Steve X. Chen, Claudia N. Dennler, Vivian T. Dien, Derek Fuller, Ryan Kelley, Omid Khandan, Michael G. Klein, Michael Kim, Bryan R. Lajoie, Bill Lin, Yu Liu, Tyler Lopez, Peter T. Mains, Andrew D. Price, Samantha R. Robertson, Hermes Taylor-Weiner, Ramreddy Tippana, Austin B. Tomaney, Su Zhang, Mark R. Ambroso, Rosita Bajari, Ava M. Bellizzi, Chris B. Benitez, Daniel R. Berard, Lorenzo Berti, Kelly N. Blease, Angela P. Blum, Andrew M. Boddicker, Leo Bondar, Chris Brown, Chris A. Bui, Juan Calleja-Aguirre, Kevin Cappa, Joshua Chan, Victor W. Chang, Katherine Charov, Xiyi Chen, Rodger M. Constandse, Ryan Costello, Weston Damron, Mariam Dawood, Nicole DeBuono, John D. Dimalanta, Laure Edoli, Keerthana Elango, Nikka Faustino, Chao Feng, Mathhew Ferrari, Keith Frankie, Adam Fries, Anne Galloway, Vlad Gavrila, Gregory J. Gemmen, James Ghadiali, Arash Ghorbani, Logan A. Goddard, Adriana R. Guetter, Garren L. Hendricks, Jendrik Hentschel, Daniel J. Honigfort, Yun-Ting Hsieh, Yu-Hsien Hwang Fu, Scott K. Im, Chaoyi Jin, Shradha Kabu, Daniel E. Kincade, Shawn Levy, Yu Li, Vincent K. Liang, William H. Light, Jonathan B. Lipsher, Tsung-li Liu, Grace Long, Rui Ma, John M. Mailloux, Kyle A. Mandla, Anyssa R. Martinez, Max Mass, Daniel T. McKean, Michael Meron, Celyne S. Moh, Rachel K. Moore, Juan Moreno, Jordan M. Neysmith, Cassandra S. Niman, Jesus M. Nunez, Micah T. Ojeda, Sara Espinosa Ortiz, Jenna Owens, Geoffrey Piland, Daniel J. Proctor, Josua B. Purba, Michael Ray, Daisong Rong, Virginia M. Saade, Sanchari Saha, Gustav Santo Tomas, Nicholas Scheidler, Luqmanal H. Sirajudeen, Samantha Snow, Gudrun Stengel, Ryan Stinson, Michael J. Stone, Keoni J. Sundseth, Eileen Thai, Connor J. Thompson, Marco Tjioe, Christy L. Trejo, Greg Trieger, Diane Ni Truong, Ben Tse, Benjamin Voiles, Henry Vuong, Jennifer C. Wong, Chiung-Ting Wu, Hua Yu, Yingxian Yu, Ming Yu, Xi Zhang, Da Zhao, Genhua Zheng, Molly He, Michael Previte
We present avidity sequencing - a novel sequencing chemistry that separately optimizes the process of stepping along a DNA template and the process of identifying each nucleotide within the template. Nucleotide identification uses multivalent nucleot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::00c30543f0516bc520d95458ddea143a
https://doi.org/10.1101/2022.11.03.514117
https://doi.org/10.1101/2022.11.03.514117
Autor:
Yuka E. Lewis, Balyn W. Zaro, Maxwell Taylor Roth, Don B. Arnold, Nicholas P. Marotta, Mark R. Ambroso, Yu Hsuan Lin, Matthew R. Pratt, Ralf Langen
Publikováno v:
Nature chemistry, vol 7, iss 11
Several aggregation-prone proteins associated with neurodegenerative diseases can be modified by O-linked N-acetyl-glucosamine (O-GlcNAc) in vivo. One of these proteins, α-synuclein, is a toxic aggregating protein associated with synucleinopathies,
Publikováno v:
Proceedings of the National Academy of Sciences. 111:6982-6987
Membrane remodeling is controlled by proteins that can promote the formation of highly curved spherical or cylindrical membranes. How a protein induces these different types of membrane curvature and how cells regulate this process is still unclear.
Publikováno v:
Methods in enzymology. 564
Endocytosis and other membrane remodeling processes require the coordinated generation of different membrane shapes. Proteins capable of manipulating lipid bilayers mediate these events using mechanisms that are not fully understood. Progress is limi
Endocytosis and other membrane remodeling processes require the coordinated generation of different membrane shapes. Proteins capable of manipulating lipid bilayers mediate these events using mechanisms that are not fully understood. Progress is limi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0ae19287b7c38729d422b39523d6903b
https://doi.org/10.1016/bs.mie.2015.07.002
https://doi.org/10.1016/bs.mie.2015.07.002
Publikováno v:
Structure (London, England : 1993). 23(5)
SummaryBAR proteins are involved in a variety of membrane remodeling events but how they can mold membranes into different shapes remains poorly understood. Using electron paramagnetic resonance, we find that vesicle binding of the N-BAR protein amph
Hydration dynamics as an intrinsic ruler for refining protein structure at lipid membrane interfaces
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 110, iss 42
Knowing the topology and location of protein segments at water-membrane interfaces is critical for rationalizing their functions, but their characterization is challenging under physiological conditions. Here, we debut a unique spectroscopic approach