Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Harshal A. Chokhawala"'
Autor:
Richard Schwab, Ajit Varki, Xi Chen, Karen Messer, Yu-Tsueng Liu, Inder M. Verma, Darius Ghaderi, Oded Singer, Dinorah Friedmann-Morvinski, Patrick Secrest, Hongzhi Cao, Harshal A. Chokhawala, Saddam Muthana, Shengshu Huang, Hai Yu, Minya Pu, Nancy Hurtado-Ziola, Vered Padler-Karavani
Supplementary Figures 1-4, Tables 1-2 from Human Xeno-Autoantibodies against a Non-Human Sialic Acid Serve as Novel Serum Biomarkers and Immunotherapeutics in Cancer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d3e4ac08ea8fef06a087815915a6137
https://doi.org/10.1158/0008-5472.22392473
https://doi.org/10.1158/0008-5472.22392473
Autor:
Harvey W. Blanch, Douglas S. Clark, Alexandra Dotson-Fagerstrom, Craig M. Dana, Harshal A. Chokhawala, Sarala M. Kal, Christine M. Roche
Publikováno v:
Biotechnology and Bioengineering. 111:842-847
The commercialization of lignocellulosic biofuels relies in part on the ability to engineer cellulase enzymes to have properties compatible with practical processing conditions. The cellulase Cel7A has been a common engineering target because it is p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36d162b55c477730d62feb7a1d16c860
https://doi.org/10.1002/bit.25178
https://doi.org/10.1002/bit.25178
Autor:
Hongzhi Cao, David F. Smith, Haojie Zheng, Vinod K. Tiwari, Mary M. Tappert, Gillian M. Air, Yi Lasanajak, Richard D. Cummings, Xuezheng Song, Xi Chen, Harshal A. Chokhawala, Hai Yu
Publikováno v:
Journal of Biological Chemistry. 286:31610-31622
Many glycan-binding proteins in animals and pathogens recognize sialic acid or its modified forms, but their molecular recognition is poorly understood. Here we describe studies on sialic acid recognition using a novel sialylated glycan microarray co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f749f691487a4fe3821ddc001002c29f
https://doi.org/10.1074/jbc.m111.274217
https://doi.org/10.1074/jbc.m111.274217
Publikováno v:
Biochemical and Biophysical Research Communications. 361:555-560
Haemophilus ducreyi is a Gram-negative bacterium that causes chancroid, a sexually transmitted genital ulcer disease. Different lipooligosaccharide (LOS) structures have been identified from H. ducreyi strain 35000, including those sialylated glycofo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f1eeb5862190990b4ce6ed408df7df9
https://doi.org/10.1016/j.bbrc.2007.07.063
https://doi.org/10.1016/j.bbrc.2007.07.063
Autor:
Laura Ng, Lisheng Ni, Xi Chen, Harshal A. Chokhawala, Shengshu Huang, Hongzhi Cao, Andrew J. Fisher, Ryan Henning, Hai Yu
Publikováno v:
Biochemistry. 46:6288-6298
Sialyltransferases are key enzymes involved in the biosynthesis of biologically and pathologically important sialic acid-containing molecules in nature. Binary X-ray crystal structures of a multifunctional Pasteurella multocida sialyltransferase (Del
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ae4bd6f464e543c5f08734c2d3121bd
https://doi.org/10.1021/bi700346w
https://doi.org/10.1021/bi700346w
Publikováno v:
ChemBioChem. 8:194-201
Sialidases, or neuraminidases, are enzymes that cleave terminal sialic acid (Sia) residues from complex sialic acid-containing structures. They have been found in many animals and microorganisms and are important in various physiological and patholog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::129b1889ba9fe4ac13c6ae4b595bbcfe
https://doi.org/10.1002/cbic.200600410
https://doi.org/10.1002/cbic.200600410
Publikováno v:
Biochemistry. 45:2139-2148
Sialyltransferases catalyze reactions that transfer a sialic acid from CMP-sialic acid to an acceptor (a structure terminated with galactose, N-acetylgalactosamine, or sialic acid). They are key enzymes that catalyze the synthesis of sialic acid-cont
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4bf20831dd165b687b0260d61fe9fba2
https://doi.org/10.1021/bi0524013
https://doi.org/10.1021/bi0524013
Autor:
Meera E. Atreya, Craig M. Dana, Douglas S. Clark, Neeraja Vegesna, Harvey W. Blanch, Christine M. Roche, Tae-Wan Kim, Harshal A. Chokhawala
Publikováno v:
BMC Biotechnology
BMC biotechnology, vol 15, iss 1
BMC biotechnology, vol 15, iss 1
Background Trichoderma reesei is a key cellulase source for economically saccharifying cellulosic biomass for the production of biofuels. Lignocellulose hydrolysis at temperatures above the optimum temperature of T. reesei cellulases (~50°C) could p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82ba75a72f6bcd71fd9071d7e2c3a4fe
https://pubmed.ncbi.nlm.nih.gov/25879765
https://pubmed.ncbi.nlm.nih.gov/25879765
Autor:
Yiyan Fei, Hai Yu, Kam Lau, Xiangdong Zhu, Yanhong Li, Xi Chen, Harshal A. Chokhawala, J. P. Landry, Shengshu Huang
Publikováno v:
The Review of scientific instruments, vol 84, iss 11
A biological state is equilibrium of multiple concurrent biomolecular reactions. The relative importance of these reactions depends on physiological temperature typically between 10 °C and 50 °C. Experimentally the temperature dependence of binding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::778348459dfd150a532117f36ea17e56
https://escholarship.org/uc/item/6j59v4p0
https://escholarship.org/uc/item/6j59v4p0
Autor:
Douglas S. Clark, Zachary M. Carrico, Sonny C. Hsiao, Michelle E. Farkas, Matthew B. Francis, Harshal A. Chokhawala, James D. Marks, Yu Zhou
Publikováno v:
ACS nano, vol 6, iss 8
We report a convenient new technique for the labeling of filamentous phage capsid proteins. Previous reports have shown that phage coat protein residues can be modified, but the lack of chemically distinct amino acids in the coat protein sequences ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2628c03f7b26dd25bcba65bd99129e7a
https://escholarship.org/uc/item/3wc3p68q
https://escholarship.org/uc/item/3wc3p68q