Výsledky vyhledávání - "Erik A. Feldmann"

The Solution Structures and Interaction of SinR and SinI: Elucidating the Mechanism of Action of the Master Regulator Switch for Biofilm Formation in Bacillus subtilis

Autor: Morgan E. Milton, Michael T. Santoro, Benjamin G. Bobay, Katherine H. Myers, Daniel B. Kearns, John Cavanagh, Sean D. Stowe, Andrew L. Olson, Richele J. Thompson, Erik A. Feldmann, G. Logan Draughn

Publikováno v: J Mol Biol

Bacteria have developed numerous protection strategies to ensure survival in harsh environments, with perhaps the most robust method being the formation of a protective biofilm. In biofilms, bacterial cells are embedded within a matrix that is compos

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b32ca89d60e7f6652ade3872b4d4903c
https://doi.org/10.1016/j.jmb.2019.08.019

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The Structure of the Biofilm-controlling Response Regulator BfmR from Acinetobacter baumannii Reveals Details of Its DNA-binding Mechanism

Autor: John Cavanagh, Morgan E. Milton, G. Logan Draughn, Braden M. Roth, Erik A. Feldmann, Luis A. Actis, Andrew L. Olson, Benjamin G. Bobay, Richele J. Thompson, Christopher Davies

Publikováno v: Journal of Molecular Biology. 430:806-821

The rise of drug-resistant bacterial infections coupled with decreasing antibiotic efficacy poses a significant challenge to global health care. Acinetobacter baumannii is an insidious, emerging bacterial pathogen responsible for severe nosocomial in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad360a1a9a1e8aa0d2a967bc91010df2
https://doi.org/10.1016/j.jmb.2018.02.002

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Structure of the Francisella response regulator QseB receiver domain, and characterization of QseB inhibition by antibiofilm 2-aminoimidazole-based compounds

Autor: Richele J. Thompson, Daina Zeng, David K. Jung, John Cavanagh, Kelly E. Theisen, C. Leigh Allen, Christian Melander, Roberta J. Melander, Erik A. Feldmann, Matthew D. Stephens, Morgan E. Milton, Benjamin G. Bobay

Publikováno v: Molecular Microbiology. 106:223-235

With antibiotic resistance increasing at alarming rates, targets for new antimicrobial therapies must be identified. A particularly promising target is the bacterial two-component system. Two-component systems allow bacteria to detect, evaluate and p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::52b9eb78320323ad709a23687c2355c9
https://doi.org/10.1111/mmi.13759

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Structure of the Francisella response regulator QseB receiver domain, and characterization of QseB inhibition by antibiofilm 2-aminoimidazole-based compounds

Autor: Morgan E, Milton, C Leigh, Allen, Erik A, Feldmann, Benjamin G, Bobay, David K, Jung, Matthew D, Stephens, Roberta J, Melander, Kelly E, Theisen, Daina, Zeng, Richele J, Thompson, Christian, Melander, John, Cavanagh

Publikováno v: Molecular microbiology. 106(2)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6fadef20ef5005c66840a96803a0f922
https://pubmed.ncbi.nlm.nih.gov/28755524

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The DNA-Binding Domain of Yeast Rap1 Interacts with Double-Stranded DNA in Multiple Binding Modes

Autor: Erik A. Feldmann, Roberto Galletto

Publikováno v: Biochemistry

Saccharomyces cerevisiae repressor-activator protein 1 (Rap1) is an essential protein involved in multiple steps of DNA regulation, as an activator in transcription, as a repressor at silencer elements, and as a major component of the shelterin-like

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac9497b36cdc8f471c995faccaf24c9a
http://europepmc.org/articles/PMC4263426

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Solution NMR structures provide first structural coverage of the large protein domain family PF08369 and complementary structural coverage of dark operative protochlorophyllide oxidoreductase complexes

Autor: Erik A. Feldmann, John Everett, Michael A. Kennedy, Yunfen He, Alexander Eletsky, Thomas Acton, Gaetano T. Montelione, Rong Xiao, Thomas Szyperski, Surya V.S.R.K. Pulavarti

Publikováno v: Journal of Structural and Functional Genomics. 14:119-126

High-quality NMR structures of the C-terminal domain comprising residues 484-537 of the 537-residue protein Bacterial chlorophyll subunit B (BchB) from Chlorobium tepidum and residues 9-61 of 61-residue Asr4154 from Nostoc sp. (strain PCC 7120) exhib

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c6c6650418f84fad783d3d2abab04e7
https://doi.org/10.1007/s10969-013-9159-5

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Differential Binding between PatS C-Terminal Peptide Fragments and HetR from Anabaena sp. PCC 7120

Autor: Sean M. Callahan, Robert M. McCarrick, Clay H. J. Mishler, Indra D. Sahu, Shuisong Ni, Blanton S. Tolbert, Yegor Kushnir, Gary A. Lorigan, Erik A. Feldmann, Michael A. Kennedy, Jeffrey D. Levengood

Publikováno v: Biochemistry. 51:2436-2442

Heterocyst differentiation in the filamentous cyanobacterium Anabaena sp. strain PCC 7120 occurs at regular intervals under nitrogen starvation and is regulated by a host of signaling molecules responsive to availability of fixed nitrogen. The hetero

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32d008187b28412a979fb95f4a0ac537
https://doi.org/10.1021/bi300228n

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Solution NMR structure of Asl3597 from Nostoc sp. PCC7120, the first structure from protein domain family PF12095, reveals a novel fold

Autor: John Everett, Michael A. Kennedy, Rong Xiao, Yunhuang Yang, Theresa Ramelot, Gaetano T. Montelione, Thomas Acton, Erik A. Feldmann

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 80:671-675

The protein domain family PF12095 (DUF3571) is a functionally uncharacterized family of small proteins conserved from cyanobacteria to plants that are typically 85 to 95 amino acids in length in cyanobacteria. In this report, we describe the solution

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f3ef77946e757a9e134f822c2d452d7
https://doi.org/10.1002/prot.23236

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Combining NMR and EPR Methods for Homodimer Protein Structure Determination

Autor: Haleema Janjua, Thomas Acton, Huang Wang, Erik A. Feldmann, M.A. Kennedy, Gaetano T. Montelione, Mei Jiang, Shuisong Ni, Rong Xiao, Robert M. McCarrick, Yunhuang Yang, John K. Everett, John R. Cort, Theresa Ramelot, Colleen Ciccosanti

Publikováno v: Journal of the American Chemical Society. 132:11910-11913

There is a general need to develop more powerful and more robust methods for structural characterization of homodimers, homo-oligomers, and multiprotein complexes using solution-state NMR methods. In recent years, there has been increasing emphasis o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7ac0642c99787449da52e4c1580549a
https://doi.org/10.1021/ja105080h

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