Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Mengxuan JIA"'
Publikováno v:
Meitan kexue jishu, Vol 52, Iss 8, Pp 209-221 (2024)
At present, the construction of ecological civilisation and the goal of carbon neutrality have become national strategies, which require the ecological restoration of mines to develop in a green, coordinated and sustainable direction.The integration
Externí odkaz:
https://doaj.org/article/686e51e4c20c485faeacafb9a6c63d37
Autor:
Samantha H. Sarni, Jorjethe Roca, Chen Du, Mengxuan Jia, Hantian Li, Ana Damjanovic, Ewelina M. Małecka, Vicki H. Wysocki, Sarah A. Woodson
RNA-binding proteins contain intrinsically disordered regions whose functions in RNA recognition are poorly understood. The RNA chaperone Hfq is a homohexamer that contains six flexible C-terminal domains (CTDs). The effect of the CTDs on Hfq’s int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3675a61cb0e5842187d8cb2dc79d617
https://doi.org/10.1101/2022.05.23.493136
https://doi.org/10.1101/2022.05.23.493136
Autor:
Matthew S. Wilken, Florian Busch, Zibo Chen, Ryan Kibler, Galen Dods, Vicki H. Wysocki, Christie Ciarlo, Mengxuan Jia, Hanna Liao, Michael C. Jewett, John A. Stamatoyannopoulos, Jocelynn R. Pearl, Basile I. M. Wicky, Shon Green, David Baker, Zachary L. VanAernum, Hana El-Samad, Scott E. Boyken, Andrew Hunt
Publikováno v:
Science
Designer gates Signaling in cells can occur through protein-protein interactions. Chen et al. describe the design of logic gates that can regulate protein association. The gates were built from small, designed proteins that all have a similar structu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de8ef1f35b344f8981120798e53c38a6
https://doi.org/10.1126/science.aay2790
https://doi.org/10.1126/science.aay2790
Autor:
Florian Busch, Vicki H. Wysocki, Benjamin J. Jones, Mengxuan Jia, Zachary L. VanAernum, David Baker, Scott E. Boyken, Aniruddha Sahasrabuddhe, Zibo Chen
Publikováno v:
Nat Protoc
It is important to assess the identity and purity of proteins and protein complexes during and after protein purification to ensure that samples are of sufficient quality for further biochemical and structural characterization, as well as for use in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa83cf74dfd22642c7d7f91504e03f67
https://doi.org/10.1038/s41596-019-0281-0
https://doi.org/10.1038/s41596-019-0281-0
Autor:
Mengxuan Jia, David Flores-Solis, David Baker, Scott E. Boyken, Zibo Chen, T. J. Brunette, Matthew J. Bick, Sherry Bermeo, Aniruddha Sahasrabuddhe, Frank DiMaio, Vicki H. Wysocki, Peilong Lu, Nikolaos G. Sgourakis, Florian Busch, Robert A. Langan, Vikram Khipple Mulligan, Lauren Carter, Zachary L. VanAernum
Publikováno v:
Nature. 565:106-111
Heterodimeric interaction specificity between two DNA strands, and between protein and DNA, is often achieved by varying side chains or bases coming off the protein or DNA backbone -- for example, the bases participating in Watson-Crick base pairing
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6990e1e7e7b90f1dd2b5343b33b7a017
https://doi.org/10.1038/s41586-018-0802-y
https://doi.org/10.1038/s41586-018-0802-y
Autor:
Sarni, Samantha H., Roca, Jorjethe, Chen Du, Mengxuan Jia, Hantian Li, Damjanovic, Ana, Małecka, Ewelina M., Wysocki, Vicki H., Woodson, Sarah A.
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America; 11/22/2022, Vol. 119 Issue 47, p1-8, 32p
Publikováno v:
International Journal of Mass Spectrometry. 471:116725
A flexible inline size exclusion chromatography (SEC) and ion-exchange chromatography (IEX) method coupled to native mass spectrometry (nMS) method was developed for the analysis of protein aggregates and charge variants in a single run of biotherape
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5e080443ce677abb71527b258dcf2c37
https://doi.org/10.1016/j.ijms.2021.116725
https://doi.org/10.1016/j.ijms.2021.116725
Autor:
James A. Cowan, Insiya Fidai, Christine Wachnowsky, Sambuddha Sen, Vicki H. Wysocki, Mengxuan Jia
Publikováno v:
Angew Chem Int Ed Engl
Many iron-sulfur proteins involved in cluster trafficking form [2Fe-2S]-cluster-bridged complexes that are often challenging to characterize because of the inherent instability of the cluster at the interface. In this work, we illustrate the use of f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07d5d2da2880a9c9e02b486ddae20a3a
https://pubmed.ncbi.nlm.nih.gov/32031732
https://pubmed.ncbi.nlm.nih.gov/32031732
Autor:
Vicki Wysocki, David Baker, Aniruddha Sahasrabuddhe, Scott E. Boyken, Zibo Chen, Mengxuan Jia, Benjamin J. Jones, Florian Busch, Zachary VanAernum
It is important to assess the identity and purity of proteins and protein complexes during and after protein purification to ensure that samples are of sufficient quality for further biochemical and structural characterization, as well as for use in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be61ffa7d185243770a50f8f2021b18e
https://doi.org/10.26434/chemrxiv.8792177.v2
https://doi.org/10.26434/chemrxiv.8792177.v2
Autor:
Vicki H. Wysocki, Aniruddha Sahasrabuddhe, David Baker, Kelly K. Lee, Banumathi Sankaran, Zibo Chen, Kathy Y. Wei, Mengxuan Jia, Scott E. Boyken, Alexander Mileant, Carl Walkey, Florian Busch, Edgar A. Hodge, Neil P. King, Alfredo Quijano-Rubio, Mark A. Benhaim, Heejun Choi, Sarah Byron, Jason C. Klima, Jennifer Lippincott-Schwartz, Matthew J. Bick
Publikováno v:
Science (New York, N.Y.), vol 364, iss 6441
The ability of naturally occurring proteins to change conformation in response to environmental changes is critical to biological function. Although there have been advances in the de novo design of stable proteins with a single, deep free-energy min
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5030e7a5392e3879c069d3defb8f4d22
https://pubmed.ncbi.nlm.nih.gov/31097662
https://pubmed.ncbi.nlm.nih.gov/31097662