Zobrazeno 1 - 10
of 84
pro vyhledávání: '"Paul Gollnick"'
Autor:
Craig A. McElroy, Elihu C. Ihms, Deepak Kumar Yadav, Melody L. Holmquist, Vibhuti Wadhwa, Vicki H. Wysocki, Paul Gollnick, Mark P. Foster
Publikováno v:
Journal of Structural Biology: X, Vol 10, Iss , Pp 100103- (2024)
Cellular production of tryptophan is metabolically expensive and tightly regulated. The small Bacillus subtilis zinc binding Anti-TRAP protein (AT), which is the product of the yczA/rtpA gene, is upregulated in response to accumulating levels of unch
Externí odkaz:
https://doaj.org/article/97ca08ddeeaa4d86bfaef1e8ed2b514e
Autor:
Natalie M McAdams, Paul Gollnick
Publikováno v:
PLoS ONE, Vol 9, Iss 2, p e88097 (2014)
In Bacillus subtilis, transcription of the tryptophan biosynthetic operon is regulated by an attenuation mechanism. When intracellular tryptophan levels are high, the TRAP protein binds to the 5' leader region of the nascent trp mRNA and induces tran
Externí odkaz:
https://doaj.org/article/3c48bbe2fe3a4b9db348185d96e5b8a8
Autor:
Oliver W Bayfield, Chao-Sheng Chen, Andrea R Patterson, Weisha Luan, Callum Smits, Paul Gollnick, Alfred A Antson
Publikováno v:
PLoS ONE, Vol 7, Iss 9, p e44309 (2012)
Subunit number is amongst the most important structural parameters that determine size, symmetry and geometry of a circular protein oligomer. The L-tryptophan biosynthesis regulator, TRAP, present in several Bacilli, is a good model system for invest
Externí odkaz:
https://doaj.org/article/a858ee0d002a4c28b915b213ccab8aa6
Autor:
Chao-Sheng Chen, Callum Smits, Guy G Dodson, Mikhail B Shevtsov, Natalie Merlino, Paul Gollnick, Alfred A Antson
Publikováno v:
PLoS ONE, Vol 6, Iss 10, p e25296 (2011)
Many critical cellular functions are performed by multisubunit circular protein oligomers whose internal geometry has evolved to meet functional requirements. The subunit number is arguably the most critical parameter of a circular protein assembly,
Externí odkaz:
https://doaj.org/article/f7801003277d4445899bdce6414be90e
Autor:
Andrew Norris, Katie Lichtenthal, Mark Foster, Skyler Kelly, Paul Gollnick, Vicki Wysocki, Elihu Ihms, Weicheng Li
Publikováno v:
Protein science : a publication of the Protein Society. 31(10)
Homo-oligomeric ligand-activated proteins are ubiquitous in biology. The functions of such molecules are commonly regulated by allosteric coupling between ligand-binding sites. Understanding the basis for this regulation requires both quantifying the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c6fe445805c367c87ef87e451019b0b
https://pubmed.ncbi.nlm.nih.gov/36173171
https://pubmed.ncbi.nlm.nih.gov/36173171
Publikováno v:
Biochemistry
Allostery pervades macromolecular function and drives cooperative binding of ligands to macromolecules. To decipher the mechanisms of cooperative ligand binding it is necessary to define, at a microscopic level, the thermodynamic consequences of bind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cc82a65bc493ffe7a2ac4184a741994
https://doi.org/10.1021/acs.biochem.0c00352
https://doi.org/10.1021/acs.biochem.0c00352
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Scientific Reports
Scientific Reports
Methanothermobacter thermoautotrophicus RNA ligase (MthRnl) catalyzes formation of phosphodiester bonds between the 5′-phosphate and 3′-hydroxyl termini of single-stranded RNAs. It can also react with RNA with a 3′-phosphate end to generate a 2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b9666b802450ea251304b489cf625f1
http://link.springer.com/article/10.1038/s41598-017-11693-0
http://link.springer.com/article/10.1038/s41598-017-11693-0
Mechanistic Models Fit to Variable Temperature Calorimetric Data Provide Insights into Cooperativity
Publikováno v:
Biophysical Journal. 112:1328-1338
Allostery pervades macromolecular function and drives cooperative binding of ligands to macromolecules. To decipher the mechanisms of cooperative ligand binding it is necessary to define at a microscopic level the structural and thermodynamic consequ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4646437a78f89d4411597c6df4e73e57
https://doi.org/10.1016/j.bpj.2017.02.031
https://doi.org/10.1016/j.bpj.2017.02.031
Autor:
Anna V. Ignatochkina, C. Kiong Ho, Paul Gollnick, Raka Ghosh, Katsuhiko S. Murakami, Shigeo Yoshinari, Huiqiong Gu
Publikováno v:
Nucleic Acids Research
An ATP-dependent RNA ligase from Methanobacterium thermoautotrophicum (MthRnl) catalyzes intramolecular ligation of single-stranded RNA to form a closed circular RNA via covalent ligase-AMP and RNA-adenylylate intermediate. Here, we report the X-ray
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc3528cdcb0b017468a258fc118ab98d
https://doi.org/10.1093/nar/gkw094
https://doi.org/10.1093/nar/gkw094
Autor:
Paul Gollnick, Amber N. Shatzer, Richard C. Condit, Susan M. D'Costa, Baron McFadden, Jessica Tate, Nicholas M. Lewandowski, Rachel L. Boldt
Publikováno v:
Virology. 487:27-40
Prior biochemical analysis of the heterodimeric vaccinia virus mRNA capping enzyme suggests roles not only in mRNA capping but also in early viral gene transcription termination and intermediate viral gene transcription initiation. Prior phenotypic c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae300b39983707ea1ca7dfab58dbe3a0
https://doi.org/10.1016/j.virol.2015.10.011
https://doi.org/10.1016/j.virol.2015.10.011