Zobrazeno 1 - 10
of 284
pro vyhledávání: '"Douglas C Rees"'
Autor:
Aaron L Nichols, Zack Blumenfeld, Chengcheng Fan, Laura Luebbert, Annet EM Blom, Bruce N Cohen, Jonathan S Marvin, Philip M Borden, Charlene H Kim, Anand K Muthusamy, Amol V Shivange, Hailey J Knox, Hugo Rego Campello, Jonathan H Wang, Dennis A Dougherty, Loren L Looger, Timothy Gallagher, Douglas C Rees, Henry A Lester
Publikováno v:
eLife, Vol 11 (2022)
Externí odkaz:
https://doaj.org/article/098460172c5e405ebfd89ac4744a4398
Publikováno v:
eLife, Vol 11 (2022)
The nitrogenase Fe protein mediates ATP-dependent electron transfer to the nitrogenase MoFe protein during nitrogen fixation, in addition to catalyzing MoFe protein-independent substrate (CO2) reduction and facilitating MoFe protein metallocluster bi
Externí odkaz:
https://doaj.org/article/85234b48d7804c00a450ffc97fcb778f
Autor:
Chengcheng Fan, Douglas C Rees
Publikováno v:
eLife, Vol 11 (2022)
The ATP binding cassette (ABC) transporter of mitochondria (Atm) from Arabidopsis thaliana (AtAtm3) has been implicated in the maturation of cytosolic iron-sulfur proteins and heavy metal detoxification, plausibly by exporting glutathione derivatives
Externí odkaz:
https://doaj.org/article/1697e455bdbb4a5d95fc038613f1e3a7
Autor:
Aaron L Nichols, Zack Blumenfeld, Chengcheng Fan, Laura Luebbert, Annet EM Blom, Bruce N Cohen, Jonathan S Marvin, Philip M Borden, Charlene H Kim, Anand K Muthusamy, Amol V Shivange, Hailey J Knox, Hugo Rego Campello, Jonathan H Wang, Dennis A Dougherty, Loren L Looger, Timothy Gallagher, Douglas C Rees, Henry A Lester
Publikováno v:
eLife, Vol 11 (2022)
Nicotinic partial agonists provide an accepted aid for smoking cessation and thus contribute to decreasing tobacco-related disease. Improved drugs constitute a continued area of study. However, there remains no reductionist method to examine the cell
Externí odkaz:
https://doaj.org/article/4b4e86491b454335b0724b76381431a8
Autor:
Naima G Sharaf, Mona Shahgholi, Esther Kim, Jeffrey Y Lai, David G VanderVelde, Allen T Lee, Douglas C Rees
Publikováno v:
eLife, Vol 10 (2021)
NmMetQ is a substrate-binding protein (SBP) from Neisseria meningitidis that has been identified as a surface-exposed candidate antigen for meningococcal vaccines. However, this location for NmMetQ challenges the prevailing view that SBPs in Gram-neg
Externí odkaz:
https://doaj.org/article/644cf02d64a6410194394509bed6ace7
Autor:
Aaron J Fisher, Rodolfo Mendoza-Denton, Colette Patt, Ira Young, Andrew Eppig, Robin L Garrell, Douglas C Rees, Tenea W Nelson, Mark A Richards
Publikováno v:
PLoS ONE, Vol 14, Iss 1, p e0209279 (2019)
The advancement of underrepresented minority and women PhD students to elite postdoctoral and faculty positions in the STEM fields continues to lag that of majority males, despite decades of efforts to mitigate bias and increase opportunities for stu
Externí odkaz:
https://doaj.org/article/c92ad7af8708407da56815b06f128f60
Autor:
Lorenz Heidinger, Kathryn Perez, Thomas Spatzal, Oliver Einsle, Stefan Weber, Douglas C. Rees, Erik Schleicher
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-15 (2024)
Abstract Due to the complexity of the catalytic FeMo cofactor site in nitrogenases that mediates the reduction of molecular nitrogen to ammonium, mechanistic details of this reaction remain under debate. In this study, selenium- and sulfur-incorporat
Externí odkaz:
https://doaj.org/article/3533319ff4c04865b13a91688453b6fa
Publikováno v:
eLife, Vol 4 (2015)
Dinitrogen reduction in the biological nitrogen cycle is catalyzed by nitrogenase, a two-component metalloenzyme. Understanding of the transformation of the inert resting state of the active site FeMo-cofactor into an activated state capable of reduc
Externí odkaz:
https://doaj.org/article/0cdb2a0894bb42d2ba78050463fd7b8d
Publikováno v:
PLoS ONE, Vol 8, Iss 9, p e72751 (2013)
Amino acid residues critical for a protein's structure-function are retained by natural selection and these residues are identified by the level of variance in co-aligned homologous protein sequences. The relevant residues in the nitrogen fixation Co
Externí odkaz:
https://doaj.org/article/3603777c621042f3a66a83315c82155f
Publikováno v:
PLoS Biology, Vol 2, Iss 1, p E2 (2004)
The JAMM (JAB1/MPN/Mov34 metalloenzyme) motif in Rpn11 and Csn5 underlies isopeptidase activities intrinsic to the proteasome and signalosome, respectively. We show here that the archaebacterial protein AfJAMM possesses the key features of a zinc met
Externí odkaz:
https://doaj.org/article/925701d1c95c403d8e24da88cc6d57b5