Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Jarmila Jancarik"'
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63:369-374
Using single-wavelength anomalous dispersion data obtained from a gold-derivatized crystal, the X-ray crystal structure of the protein 067745_AQUAE from the prokaryotic organism Aquifex aeolicus has been determined to a resolution of 2.0 A. Amino-aci
Autor:
Marc Whitlow, Sung-Hou Kim, Jarmila Jancarik, David D. Davey, David R. Light, Marc Adler, Gary Phillips, Galina Rumennik
Publikováno v:
Biochemistry. 39:12534-12542
Factor Xa plays a critical role in the formation of blood clots. This serine protease catalyzes the conversion of prothrombin to thrombin, the first joint step that links the intrinsic and extrinsic coagulation pathways. There is considerable interes
Autor:
Kirston E. Koths, Sung-Hou Kim, Robert Halenbeck, Jarmila Jancarik, Jayvardhan Pandit, Andrew Bohm
Publikováno v:
Science. 258:1358-1362
Macrophage colony-stimulating factor (M-CSF) triggers the development of cells of the monocyte-macrophage lineage and has a variety of stimulatory effects on mature cells of this class. The biologically active form of M-CSF is a disulfide-linked dime
Autor:
Axel T. Brunger, Eiko Ohtsuka, Jarmila Jancarik, Sung-Hou Kim, Susumu Nishimura, Abraham M. deVos, Liang Tong, Ziro Yamaizumi, M. V. Milburn
Publikováno v:
Proceedings of the National Academy of Sciences. 87:4849-4853
Normal RAS proteins play a key role of molecular switch in the transduction of the growth signal from extracellular to intracellular space. The state of the switch is "on" when GTP is bound and "off" when GDP is bound to the protein. The crystal stru
Autor:
Hisao Yokota, Sung-Hou Kim, Rosalind Kim, Yun Lou, Alexander F. Yakunin, Paul D. Adams, Qian Steven Xu, Kate Kuznetsova, Jarmila Jancarik
Publikováno v:
Journal of structural and functional genomics. 6(4)
Phosphotransacetylase (Pta) [EC 2.3.1.8] plays a major role in acetate metabolism by catalyzing the reversible transfer of the acetyl group between coenzyme A (CoA) and orthophosphate: CH3COSCoA+HPO $$_{4}^{2-}\rightleftarrows$$ CH3COOPO 3 2− +CoAS
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 60(Pt 9)
One of the most critical steps in the preparation of protein samples for structural studies by X-ray crystallography is to obtain biochemically pure and conformationally homogenous protein samples. Very often, the purified sample does not meet these
Publikováno v:
Journal of molecular biology. 230(4)
The major transitions of the eukaryotic cell cycle are triggered by cyclin-dependent protein kinases. We report the purification and crystallization of the catalytic subunit of human cyclin-dependent kinase 2 (CDK2), which has been implicated in the
Autor:
M. V. Milburn, Sung-Hou Kim, Daniel E. Koshland, Daniel L. Milligan, William G. Scott, Gilbert G. Privé, Joanne Yeh, Jarmila Jancarik
Publikováno v:
Science (New York, N.Y.), vol 254, iss 5036
Milburn, MV; Privé, GG; Milligan, DL; Scott, WG; Yeh, J; Jancarik, J; et al.(1991). Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science, 254(5036), 1342-1347. doi: 10.1126/science.1660187. UC Santa Cruz: Retrieved from: http://www.escholarship.org/uc/item/5h52w0jp
Milburn, MV; Privé, GG; Milligan, DL; Scott, WG; Yeh, J; Jancarik, J; et al.(1991). Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science, 254(5036), 1342-1347. doi: 10.1126/science.1660187. UC Santa Cruz: Retrieved from: http://www.escholarship.org/uc/item/5h52w0jp
The three-dimensional structure of an active, disulfide cross-linked dimer of the ligand-binding domain of the Salmonella typhimurium aspartate receptor and that of an aspartate complex have been determined by x-ray crystallographic methods at 2.4 an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24b9bf149e995fc12f5f683e670f19f5
https://escholarship.org/uc/item/5h52w0jp
https://escholarship.org/uc/item/5h52w0jp
Publikováno v:
Journal of molecular biology, vol 221, iss 1
Jancarik, J; Scott, WG; Milligan, DL; Koshland, DE; & Kim, SH. (1991). Crystallization and preliminary X-ray diffraction study of the ligand-binding domain of the bacterial chemotaxis-mediating aspartate receptor of Salmonella typhimurium. Journal of Molecular Biology, 221(1), 31-34. doi: 10.1016/0022-2836(91)80198-4. UC Santa Cruz: Retrieved from: http://www.escholarship.org/uc/item/8br6883h
Jancarik, J; Scott, WG; Milligan, DL; Koshland, DE; & Kim, SH. (1991). Crystallization and preliminary X-ray diffraction study of the ligand-binding domain of the bacterial chemotaxis-mediating aspartate receptor of Salmonella typhimurium. Journal of Molecular Biology, 221(1), 31-34. doi: 10.1016/0022-2836(91)80198-4. UC Santa Cruz: Retrieved from: http://www.escholarship.org/uc/item/8br6883h
The periplasmic domain of the aspartate chemotaxis receptor from Salmonella typhimurium has been crystallized in the presence and absence of bound aspartate. Both crystal forms were grown by precipitation with lithium sulfate and diffract to 1·8 Å
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f030704ff7547b873b080dbe61e47e9e
https://escholarship.org/uc/item/8br6883h
https://escholarship.org/uc/item/8br6883h
Autor:
Sung-Hou Kim, Rosalind Kim, Jarmila Jancarik, Natalia Oganesyan, Jinyu Liu, Hisao Yokota, Dong Hae Shin
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 63:1137-1137