Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Malathy Satkunarajah"'
Autor:
Alan H. M. Wong, Aidan C. A. Tomlinson, Dongxia Zhou, Malathy Satkunarajah, Kevin Chen, Chetna Sharon, Marc Desforges, Pierre J. Talbot, James M. Rini
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
Coronaviruses have a relatively high mutation rate, potentially allowing fast adaptation to changing pressures. Here, Wong et al. provide the structure of the receptor-binding domain (RBD) of the human coronavirus HCoV-229E and its receptor and analy
Externí odkaz:
https://doaj.org/article/f6588e45349a4419aa4c7ce1d24b3317
Autor:
Zhijie Li, Michael Fischer, Malathy Satkunarajah, Dongxia Zhou, Stephen G. Withers, James M. Rini
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
POGLUT1 is a protein-O-glucosyltransferase that transfers glucose and xylose to the EGF-like domains of Notch and other signaling receptors. Here the authors report the structure of human POGLUT1 in complexes with 3 different EGF-like domains and don
Externí odkaz:
https://doaj.org/article/7319d160abf34c1da5150afd1e429e25
Publikováno v:
Nature Chemical Biology. 13:757-763
Protein O-fucosyltransferase 1 (POFUT1) fucosylates the epidermal growth factor (EGF)-like domains found in cell-surface and secreted glycoproteins including Notch and its ligands. Although Notch fucosylation is critical for development, and POFUT1 d
Autor:
Malathy Satkunarajah, James M. Rini, Kevin P. Chen, Chetna Sharon, Marc Desforges, Pierre J. Talbot, Aidan C. A. Tomlinson, Alan H. M. Wong, Dongxia Zhou
Publikováno v:
Nature Communications
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
RNA viruses are characterized by a high mutation rate, a buffer against environmental change. Nevertheless, the means by which random mutation improves viral fitness is not well characterized. Here we report the X-ray crystal structure of the recepto
Autor:
Dongxia Zhou, Stephen G. Withers, Malathy Satkunarajah, Michael Fischer, James M. Rini, Zhijie Li
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
Nature Communications
Nature Communications
Protein O-glucosyltransferase 1/Rumi-mediated glucosylation of Notch epidermal growth factor-like (EGF-like) domains plays an important role in Notch signaling. Protein O-glucosyltransferase 1 shows specificity for folded EGF-like domains, it can onl
Autor:
Liubov M. Lobanova, Alexander N. Zakhartchouk, George Mutwiri, James M. Rini, Nelson F. Eng, Malathy Satkunarajah
Publikováno v:
Vaccine. 30:3061-3067
Despite the availability of live attenuated measles virus (MV) vaccines, a large number of measles-associated deaths occur among infants in developing countries. The development of a measles subunit vaccine may circumvent the limitations associated w
Autor:
Malathy Satkunarajah, Cheryl M. Cameron, Francis A. Plummer, David J. Kelvin, John E. Pak, Alan Cochrane, Jody D. Berry, Jayaraman Seetharaman, James M. Rini, Chetna Sharon, Thierry C. Auperin
Publikováno v:
Journal of Molecular Biology
The spike (S) protein of the severe acute respiratory syndrome coronavirus (SARS-CoV) is responsible for host cell attachment and fusion of the viral and host cell membranes. Within S the receptor binding domain (RBD) mediates the interaction with an
Autor:
Jessica Wong, Desmond Persad, Aref Sassi, Joseph M. McCune, Bahareh Vali, Prameet M. Sheth, Marc Schweneker, Frederick Hecht, Brian Long, Mario A. Ostrowski, Gerald Spotts, R. Brad Jones, Lishomwa C. Ndhlovu, Martin D. Hyrcza, Joan M. Chapman, James M. Rini, Colin Kovacs, Mona R. Loutfy, Douglas F. Nixon, Feng Yun Yue, Gabor Gyenes, Aashish R. Jha, Tae-Wook Chun, Rupert Kaul, Roberta Halpenny, Jason D. Barbour, Malathy Satkunarajah
Publikováno v:
The Journal of Experimental Medicine
Progressive loss of T cell functionality is a hallmark of chronic infection with human immunodeficiency virus 1 (HIV-1). We have identified a novel population of dysfunctional T cells marked by surface expression of the glycoprotein Tim-3. The freque
Autor:
Malathy Satkunarajah, John E. Pak, Pascal Arnoux, Xuekun Xing, James M. Rini, Prashanth Sivarajah, Sihong Zhou
Publikováno v:
Journal of Biological Chemistry. 281:26693-26701
Leukocyte type core 2 β1,6-N-acetylglucosaminyltransferase (C2GnT-L) is a key enzyme in the biosynthesis of branched O-glycans. It is an inverting, metal ion-independent family 14 glycosyltransferase that catalyzes the formation of the core 2 O-glyc
Publikováno v:
Journal of molecular biology. 414(5)
Leukocyte-type core 2 β1,6-N-acetylglucosaminyltransferase (C2GnT-L) is an inverting, metal-ion-independent glycosyltransferase that catalyzes the formation of mucin-type core 2 O-glycans. C2GnT-L belongs to the GT-A fold, yet it lacks the metal ion