Zobrazeno 1 - 10
of 66
pro vyhledávání: '"Dennis, Carlton"'
Autor:
Stice, Dennis Carlton1, Moore, Corey L.2
Publikováno v:
Journal of Rehabilitation. Oct-Dec2005, Vol. 71 Issue 4, p12-22. 11p. 2 Charts.
Autor:
Dennis, C. C., Dennis, Carlton
Publikováno v:
Proceedings of the Annual Meeting (Western Farm Economics Association), 1966 Aug . 39, 307-312.
Externí odkaz:
https://www.jstor.org/stable/44013740
Autor:
Ian A. Wilson, Knut Jahreis, Hsiu-Ju Chiu, Mark W. Knuth, Heath E. Klock, M.A. Elsliger, Qingping Xu, Adam Godzik, Anna-Katharina Göhler, Dennis Carlton, Anne Kosfeld, Ashley M. Deacon, Mitchell D. Miller, Scott A. Lesley
Publikováno v:
Journal of Bacteriology. 194:2987-2999
MtfA of Escherichia coli (formerly YeeI) was previously identified as a regulator of the phosphoenolpyruvate (PEP)-dependent:glucose phosphotransferase system. MtfA homolog proteins are highly conserved, especially among beta- and gammaproteobacteria
Autor:
Gye Won Han, Dana Weekes, Lian Duan, Keith O. Hodgson, Polat Abdubek, Winnie W Lam, Joanna C Grant, Hsiu-Ju Chiu, Herbert L. Axelrod, Mitchell D. Miller, Dennis Carlton, Ashley M. Deacon, Anna Grzechnik, Ian A. Wilson, Christina Puckett, Sanjay Krishna, Kyle Ellrott, Mark W. Knuth, John Wooley, Abhinav Kumar, Ron Reyes, Connie Chen, Thomas Clayton, Qingping Xu, Kevin K. Jin, Henry van den Bedem, Debanu Das, Andrew P. Yeh, Tiffany Wooten, Edward Nigoghossian, Tamara Astakhova, Christine B Trame, Jiadong Zhou, Robert D. Finn, Lukasz Jaroszewski, Julie Feuerhelm, Linda Okach, Scott A. Lesley, Marc C. Deller, Andrew T. Morse, Marc André Elsliger, Constantina Bakolitsa, Xiaohui Cai, Piotr Kozbial, David Marciano, Henry J Tien, Adam Godzik, Heath E. Klock, Carol L. Farr, Amanda Nopakun, Michelle Chiu
Publikováno v:
Protein Science. 19:2131-2140
Sufu (Suppressor of Fused), a two-domain protein, plays a critical role in regulating Hedgehog signaling and is conserved from flies to humans. A few bacterial Sufu-like proteins have previously been identified based on sequence similarity to the N-t
Autor:
Mark W. Knuth, Linda Okach, Keith O. Hodgson, Winnie W Lam, Tamara Astakhova, Debanu Das, Lukasz Jaroszewski, Kevin K. Jin, Abhinav Kumar, Scott A. Lesley, Joanna C Grant, Daniel McMullan, Gye Won Han, Herbert L. Axelrod, Amanda Nopakun, Kyle Ellrott, John Wooley, Piotr Kozbial, Henry J Tien, Polat Abdubek, Christine B Trame, Ashley M. Deacon, Sanjay Krishna, Christopher L. Rife, Henry van den Bedem, Ron Reyes, Lian Duan, Dana Weekes, Adam Godzik, Heath E. Klock, Marc André Elsliger, Carol L. Farr, David Marciano, Ian A. Wilson, Julie Feuerhelm, Christina Puckett, Edward Nigoghossian, Marc C. Deller, Qingping Xu, Constantina Bakolitsa, Connie Chen, Dennis Carlton, Hsiu-Ju Chiu, Mitchell D. Miller, Anna Grzechnik, Thomas Clayton, Andrew T. Morse
Publikováno v:
Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
The crystal structure of BT_3984, a SusD-family protein, reveals a TPR N-terminal region providing support for a loop-rich C-terminal subdomain and suggests possible interfaces involved in sus complex formation.
The crystal structure of the Bact
The crystal structure of the Bact
Autor:
Andrew P. Yeh, John Wooley, Edward Nigoghossian, Qingping Xu, Christine B Trame, Gye Won Han, Kevin K. Jin, Dana Weekes, Kyle Ellrott, David Marciano, Lian Duan, Scott A. Lesley, Lukasz Jaroszewski, Debanu Das, Ashley M. Deacon, Linda Okach, Herbert L. Axelrod, Hsiu-Ju Chiu, Abhinav Kumar, Thomas Clayton, Connie Chen, Heath E. Klock, Marc André Elsliger, Carol L. Farr, Henry van den Bedem, Andrew T. Morse, Mitchell D. Miller, Anna Grzechnik, Daniel McMullan, Dennis Carlton, Keith O. Hodgson, Joanna C Grant, Winnie W Lam, Amanda Nopakun, Polat Abdubek, Tiffany Wooten, Julie Feuerhelm, Sanjay Krishna, Michelle Chiu, Adam Godzik, Marc C. Deller, Tamara Astakhova, Constantina Bakolitsa, Xiaohui Cai, Piotr Kozbial, Henry J Tien, Ron Reyes, Ian A. Wilson, Christina Puckett, Mark W. Knuth
Publikováno v:
Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
The crystal structure of BT2081 from B. thetaiotaomicron reveals a two-domain protein with a putative carbohydrate-binding site in the C-terminal domain.
BT2081 from Bacteroides thetaiotaomicron (GenBank accession code NP_810994.1) is a member
BT2081 from Bacteroides thetaiotaomicron (GenBank accession code NP_810994.1) is a member
Autor:
Lukasz Jaroszewski, Polat Abdubek, Sanjay Krishna, Adam Godzik, Henry van den Bedem, Dennis Carlton, Marc-André Elsliger, Natasha Sefcovic, Edward Nigoghossian, Piotr Kozbial, Henry J Tien, Thomas Clayton, Debanu Das, Qingping Xu, Joanna C Grant, Gye Won Han, Heath E. Klock, Carol L. Farr, Ron Reyes, Daniel McMullan, John Wooley, Hsiu-Ju Chiu, Marc C. Deller, Herbert L. Axelrod, Connie Chen, Amanda Nopakun, Tamara Astakhova, Ian A. Wilson, Kevin K. Jin, Christine B Trame, Christina Puckett, Constantina Bakolitsa, David Marciano, Keith O. Hodgson, Winnie W Lam, Ashley M. Deacon, Andrew T. Morse, Mitchell D. Miller, Anna Grzechnik, Julie Feuerhelm, Abhinav Kumar, Tiffany Wooten, Dana Weekes, Lian Duan, Linda Okach, Mark W. Knuth, Scott A. Lesley, Kyle Ellrott
Publikováno v:
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10
Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10
The first structures from the FmdE Pfam family (PF02663) reveal that some members of this family form tightly intertwined dimers consisting of two domains (N-terminal α+β core and C-terminal zinc-finger domains), whereas others contain only the cor
Autor:
Andrew T. Morse, Mark W. Knuth, Debanu Das, Marc C. Deller, John Wooley, Daniel McMullan, Dennis Carlton, Lian Duan, Dana Weekes, Ron Reyes, Heath E. Klock, Joanna C Grant, Tamara Astakhova, Adam Godzik, Gye Won Han, Kevin K. Jin, Piotr Kozbial, Henry J Tien, Julie Feuerhelm, Polat Abdubek, Hsiu-Ju Chiu, Sanjay Krishna, Edward Nigoghossian, Herbert L. Axelrod, Keith O. Hodgson, Henry van den Bedem, Ian A. Wilson, Ashley M. Deacon, Marc André Elsliger, Scott A. Lesley, Christine B Trame, David Marciano, Abhinav Kumar, Lukasz Jaroszewski, Qingping Xu, Thomas Clayton, Mitchell D. Miller, Anna Grzechnik, Linda Okach
Publikováno v:
Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
The crystal structure of the prephenate dehydrogenase component of the bifunctional H. influenzae TyrA reveals unique structural differences between bifunctional and monofunctional TyrA enzymes.
Chorismate mutase/prephenate dehydrogenase from Ha
Chorismate mutase/prephenate dehydrogenase from Ha
Autor:
Keith O. Hodgson, Kyle Ellrott, Debanu Das, Qingping Xu, Tamara Astakhova, Winnie W Lam, Polat Abdubek, Sanjay Krishna, Mark W. Knuth, Hsiu-Ju Chiu, Andrew Yeh, Jiadong Zhou, Henry van den Bedem, Lukasz Jaroszewski, Thomas Clayton, Linda Okach, Mitchell D. Miller, Anna Grzechnik, Dennis Carlton, Gye Won Han, Heath E. Klock, Abhinav Kumar, Kevin K. Jin, Edward Nigoghossian, Adam Godzik, Christine B Trame, Carol L. Farr, Andrew T. Morse, Dana Weekes, Ron Reyes, Marc C. Deller, Joanna C Grant, Scott A. Lesley, Herbert L. Axelrod, Xiaohui Cai, Piotr Kozbial, Henry J Tien, David Marciano, John Wooley, Tiffany Wooten, Lian Duan, Constantina Bakolitsa, Marc André Elsliger, Connie Chen, Julie Feuerhelm, Ashley M. Deacon, Ian A. Wilson, Christina Puckett, Amanda Nopakun
Publikováno v:
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10
Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10
The crystal structure of a novel MACPF protein, which may play a role in the adaptation of commensal bacteria to host environments in the human gut, was determined and analyzed.
Membrane-attack complex/perforin (MACPF) proteins are transmembrane
Membrane-attack complex/perforin (MACPF) proteins are transmembrane
Autor:
Gye Won Han, Mark W. Knuth, Natasha Sefcovic, Marc André Elsliger, Tamara Astakhova, Marc C. Deller, Heath E. Klock, Carol L. Farr, Xiaohui Cai, Piotr Kozbial, Adam Godzik, Thomas Clayton, Edward Nigoghossian, Qingping Xu, Ian A. Wilson, Herbert L. Axelrod, Henry J Tien, Constantina Bakolitsa, Christine B Trame, Lian Duan, Dana Weekes, Debanu Das, Daniel McMullan, Amanda Nopakun, Christina Puckett, Keith O. Hodgson, Joanna C Grant, Ron Reyes, Kevin K. Jin, David Marciano, Connie Chen, Jiadong Zhou, Dennis Carlton, Abhinav Kumar, Kyle Ellrott, Lukasz Jaroszewski, Andrew Yeh, Tiffany Wooten, Andrew T. Morse, Polat Abdubek, Michelle Chiu, Henry van den Bedem, Linda Okach, Sanjay Krishna, John Wooley, Ashley M. Deacon, Hsiu-Ju Chiu, Mitchell D. Miller, Anna Grzechnik, Scott A. Lesley, Julie Feuerhelm
Publikováno v:
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10
Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10
The crystal structure of BT1062 from Bacteroides thetaiotaomicron revealed a conserved fold that is widely adopted by fimbrial components.
BT1062 from Bacteroides thetaiotaomicron is a homolog of Mfa2 (PGN0288 or PG0179), which is a component of
BT1062 from Bacteroides thetaiotaomicron is a homolog of Mfa2 (PGN0288 or PG0179), which is a component of