Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Christopher M. DeMott"'
Autor:
Sergey Reverdatto, Christopher M. DeMott, Roxie C. Girardin, Alexander Shekhtman, David S. Burz, Jacqueline Cobbert, Kathleen A. McDonough
Publikováno v:
ACS Chemical Biology. 13:733-741
In-cell NMR spectroscopy was used to screen for drugs that disrupt the interaction between prokaryotic ubiquitin like protein, Pup, and mycobacterial proteasome ATPase, Mpa. This interaction is critical for Mycobacterium tuberculosis resistance again
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::463c8d63332fd3c622d211f882a5cccd
https://doi.org/10.1021/acschembio.7b00879
https://doi.org/10.1021/acschembio.7b00879
Publikováno v:
Biochemistry. 57:540-546
How ribosome antibiotics affect a wide range of biochemical pathways is not well understood; changes in RNA-mediated protein quinary interactions and consequent activity inside the crowded cytosol may provide one possible mechanism. We developed real
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::09cc335df9e07928d08d23c84ef6d9fe
https://doi.org/10.1021/acs.biochem.7b00938
https://doi.org/10.1021/acs.biochem.7b00938
Autor:
Sergey Reverdatto, Christopher M. DeMott, Alexander Shekhtman, David S. Burz, Subhabrata Majumder
Publikováno v:
Biochemistry. 56:4117-4126
Ribosomes are present inside bacterial cells at micromolar concentrations and occupy up to 20% of the cell volume. Under these conditions, even weak quinary interactions between ribosomes and cytosolic proteins can affect protein activity. By using i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::716cb70e1b554777b1f420fd3df5e47d
https://doi.org/10.1021/acs.biochem.7b00613
https://doi.org/10.1021/acs.biochem.7b00613
Autor:
Brian C. VanderVen, Alexander Shekhtman, Caroline Moon, Nilesh K. Banavali, Richard Johnson, Christopher M. DeMott, Christine R Montague, Kathleen A. McDonough, Guangchun Bai
Publikováno v:
Molecular Microbiology. 105:294-308
Mycobacterium tuberculosis (Mtb) uses a complex 3'-5'-cyclic AMP (cAMP) signaling network to sense and respond to changing environments encountered during infection, so perturbation of cAMP signaling might be leveraged to disrupt Mtb pathogenesis. Ho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c18d26b21ed44624557c94010196e531
https://doi.org/10.1111/mmi.13701
https://doi.org/10.1111/mmi.13701
Autor:
Leah M. Seebald, Christopher M. DeMott, Srivathsan Ranganathan, Papa Nii Asare-Okai, Anastasia Glazunova, Alan Chen, Alexander Shekhtman, Maksim Royzen
Publikováno v:
Journal of Inorganic Biochemistry. 170:202-208
Paramagnetic resonance enhancement (PRE) is an NMR technique that allows studying three-dimensional structures of RNA-protein complexes in solution. RNA strands are typically spin labeled using nitroxide reagents, which provide minimal perturbation t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2dc0910bd6456ad677195ed27a71f74d
https://doi.org/10.1016/j.jinorgbio.2017.02.024
https://doi.org/10.1016/j.jinorgbio.2017.02.024
Autor:
Christopher M. DeMott, Alexander Shekhtman, Alan A. Chen, Leah M. Seebald, Papa Nii Asare-Okai, Srivathsan V. Ranganathan, Maksim Royzen, Anastasia Glazunova
Publikováno v:
Inorganic Chemistry. 56:3773-3780
Paramagnetic NMR techniques allow for studying three-dimensional structures of RNA–protein complexes. In particular, paramagnetic relaxation enhancement (PRE) data can provide valuable information about long-range distances between different struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f4c0b026d352da92865d43278f157e5
https://doi.org/10.1021/acs.inorgchem.6b02286
https://doi.org/10.1021/acs.inorgchem.6b02286
Autor:
Christopher M. DeMott, David S. Burz, Sergey Reverdatto, Subhabrata Majumder, Alexander Shekhtman
Publikováno v:
Biochemistry. 55:4568-4573
RNA constitutes up to 20% of a cell’s dry weight, corresponding to ~20 mg/mL. This high concentration of RNA facilitates low-affinity protein–RNA quinary interactions, which may play an important role in facilitating and regulating biological pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bed32ba9bc869bb88f62d100a88e02c
https://doi.org/10.1021/acs.biochem.6b00330
https://doi.org/10.1021/acs.biochem.6b00330
Publikováno v:
Methods in Molecular Biology ISBN: 9781493973859
This paper describes three protocols for identifying interacting surfaces on 15N-labeled target proteins of known structure by using in-cell NMR spectroscopy. The first protocol describes how to identify protein quinary structure interaction surfaces
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::648648700b07402bd412fc4d8191b02e
https://doi.org/10.1007/978-1-4939-7386-6_20
https://doi.org/10.1007/978-1-4939-7386-6_20
Autor:
Richard M, Johnson, Guangchun, Bai, Christopher M, DeMott, Nilesh K, Banavali, Christine R, Montague, Caroline, Moon, Alexander, Shekhtman, Brian, VanderVen, Kathleen A, McDonough
Publikováno v:
Molecular microbiology. 105(2)
Mycobacterium tuberculosis (Mtb) uses a complex 3', 5'-cyclic AMP (cAMP) signaling network to sense and respond to changing environments encountered during infection, so perturbation of cAMP signaling might be leveraged to disrupt Mtb pathogenesis. H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f56de23ea7ae971599d23b19989ede34
https://pubmed.ncbi.nlm.nih.gov/28464471
https://pubmed.ncbi.nlm.nih.gov/28464471
Publikováno v:
ChemBioChem. 15:929-933
Distinct differences between how model proteins interact in-cell and in vitro suggest that the cytosol might have a profound effect in modulating protein-protein and/or protein-ligand interactions that are not observed in vitro. Analyses of in-cell N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be10671e65b66a07fddfd743db74e959
https://doi.org/10.1002/cbic.201400030
https://doi.org/10.1002/cbic.201400030