Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Courtni E Allen"'
Autor:
Nathan C Edwards, Zachary A Hing, Avital Perry, Adam Blaisdell, David B Kopelman, Robert Fathke, William Plum, Jordan Newell, Courtni E Allen, Geetha S, Aaron Shapiro, Chinyere Okunji, Idit Kosti, Noam Shomron, Vahan Grigoryan, Teresa M Przytycka, Zuben E Sauna, Raheleh Salari, Yael Mandel-Gutfreund, Anton A Komar, Chava Kimchi-Sarfaty
Publikováno v:
PLoS ONE, Vol 7, Iss 6, p e38864 (2012)
Synonymous variations, which are defined as codon substitutions that do not change the encoded amino acid, were previously thought to have no effect on the properties of the synthesized protein(s). However, mounting evidence shows that these "silent"
Externí odkaz:
https://doaj.org/article/1425d58426564ce68f4b13d5944197e4
Autor:
Zuben E Sauna, Chinyere Okunji, Ryan C Hunt, Tanvi Gupta, Courtni E Allen, Elizabeth Plum, Adam Blaisdell, Vahan Grigoryan, S Geetha, Robert Fathke, Kenji Soejima, Chava Kimchi-Sarfaty
Publikováno v:
PLoS ONE, Vol 4, Iss 8, p e6506 (2009)
BACKGROUND:The zinc metalloprotease ADAMTS13 is a multidomain protein that cleaves von Willebrand Factor (VWF) and is implicated in Thrombotic Thrombocytopenic Purpura (TTP) pathogenesis. Understanding the mechanism of this protein is an important go
Externí odkaz:
https://doaj.org/article/b97e435ff0124e57aef88ea631d1b582
Autor:
Neval Akbas, Courtni E. Allen, Dabney W. Dixon, Seth A. Adrian, Kenton R. Rodgers, Gudrun S. Lukat-Rodgers, Rizvan C. Uluisik, Michael P. Schmitt
Publikováno v:
Journal of Inorganic Biochemistry. 167:124-133
HtaA is a heme-binding protein that is part of the heme uptake system in Corynebacterium diphtheriae . HtaA contains two conserved regions (CR1 and CR2). It has been previously reported that both domains can bind heme; the CR2 domain binds hemoglobin
Autor:
Neval Akbas, John H. Dawson, Seth A. Adrian, Courtni E. Allen, Daniel P. Collins, Michael P. Schmitt, Gudrun S. Lukat-Rodgers, Elizabeth B. Draganova, Dabney W. Dixon, Kenton R. Rodgers
Publikováno v:
Biochemistry. 54:6598-6609
The heme uptake pathway (hmu) of Corynebacterium diphtheriae utilizes multiple proteins to bind and transport heme into the cell. One of these proteins, HmuT, delivers heme to the ABC transporter HmuUV. In this study, the axial ligation of the heme i
Publikováno v:
Journal of Bacteriology. 195:2852-2863
Corynebacterium diphtheriae utilizes hemin and hemoglobin (Hb) as iron sources during growth in iron-depleted environments, and recent studies have shown that the surface-exposed HtaA protein binds both hemin and Hb and also contributes to the utiliz
Autor:
Courtni E. Allen, Michael P. Schmitt
Publikováno v:
Journal of Bacteriology. 193:5374-5385
The human pathogen Corynebacterium diphtheriae utilizes hemin and hemoglobin as iron sources for growth in iron-depleted environments. The use of hemin iron in C. diphtheriae involves the dtxR - and iron-regulated hmu hemin uptake locus, which encode
Autor:
S Geetha, Scott L. Friedman, Elizabeth Plum, Courtni E. Allen, Zuben E. Sauna, Susan H. Garfield, Chava Kimchi-Sarfaty, Kenji Soejima, Ryan C. Hunt
Publikováno v:
Cytometry Part A. :675-681
ADAMTS13 is a secreted metalloprotease that cleaves von Willebrand Factor multimers in order to maintain proper homeostasis. A severe deficiency in ADAMTS13 triggers a disorder known as thrombotic thrombocytopenic purpura. At present, ADAMTS13 expres
Autor:
Michael P. Schmitt, Courtni E. Allen
Publikováno v:
Journal of Bacteriology. 191:2638-2648
Many human pathogens, including Corynebacterium diphtheriae , the causative agent of diphtheria, use host compounds such as heme and hemoglobin as essential iron sources. In this study, we examined the Corynebacterium hmu hemin transport region, a ge
Publikováno v:
Advanced drug delivery reviews. 55(1)
The use of pharmaceuticals during pregnancy is often a necessity for the health of the mother. Until recently, the placenta was viewed as a passive organ through which molecules are passed indiscriminately between mother and fetus. In reality, the pl
Autor:
Jordan Newell, Aaron Shapiro, Robert Fathke, Noam Shomron, Courtni E. Allen, Vahan Grigoryan, Adam Blaisdell, Zachary A. Hing, David B. Kopelman, Anton A. Komar, Zuben E. Sauna, Yael Mandel-Gutfreund, Chinyere Okunji, William Plum, Nathan C. Edwards, S Geetha, Avital Perry, Raheleh Salari, Chava Kimchi-Sarfaty, Teresa M. Przytycka, Idit Kosti
Publikováno v:
PLoS ONE
PLoS ONE, Vol 7, Iss 6, p e38864 (2012)
PLoS ONE, Vol 7, Iss 6, p e38864 (2012)
Synonymous variations, which are defined as codon substitutions that do not change the encoded amino acid, were previously thought to have no effect on the properties of the synthesized protein(s). However, mounting evidence shows that these "silent"