Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Frances A. Jurnak"'
Autor:
Xiaolin Zi, Bang H. Hoang, Dan Mercola, Frances A. Jurnak, Randall F. Holcombe, Jun Xie, Shunqiang Li, Feng Liu, Christopher Hope, Guo Yi, Wu-xiang Liao, Anne R. Simoneau, Yaxiong Tang
Epigenetic silencing of secreted wingless-type (Wnt) antagonists through hypermethylation is associated with tobacco smoking and with invasive bladder cancer. The secreted Wnt inhibitory factor-1 (WIF1) has shown consistent growth-inhibitory effect o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::043efc13b0416c7dc5a2d705d73b8803
https://doi.org/10.1158/1535-7163.c.6531509.v1
https://doi.org/10.1158/1535-7163.c.6531509.v1
Publikováno v:
Inorganic Chemistry. 14:2585-2589
Autor:
Frances A. Jurnak, Kenneth N. Raymond
Publikováno v:
Inorganic Chemistry. 13:2387-2397
Publikováno v:
Journal of Biological Chemistry. 255:6751-6757
The tetragonal crystalline form of the trypsin-treated Escherichia coli protein elongation factor Tu has been analyzed by biochemical and x-ray crystallographic techniques. The crystals contain two tightly associated polypeptide fragments of molecula
Autor:
Alexander Rich, F. Kolpak, Ian J. Molineux, Andrew H.-J. Wang, P. M.D. Fitzgerald, Frances A. Jurnak, A. McPherson
Publikováno v:
Biophysical Journal. (1):155-173
The structure of the gene 5 DNA unwinding protein from bacteriophage fd has been solved to 2.3 A resolution by x-ray diffraction techniques. The molecule contains an extensive cleft region that we have identified as the DNA binding site on the basis
Autor:
Allen Taylor, Frances A. Jurnak, Frederick H. Carpenter, Alexander Rich, Hans Bloemendal, Lucy van Loon-Klaassen
Publikováno v:
Journal of molecular biology. 112(1)
Bovine lens leucine aminopeptidase (EC no. 3.4.1.1) crystallizes in the hexagonal space group P 6 3 22 with unit cell dimensions a = 132 A and c = 122 A. The asymmetric unit consists of one protomer of molecular weight 54,000. The 32 point group symm
Publikováno v:
Chemischer Informationsdienst. 7
Publikováno v:
McPherson, A; Jurnak, FA; Wang, AHJ; Molineux, I; & Rich, A. (1979). Structure at 2.3 Å resolution of the gene 5 product of bacteriophage fd: A DNA unwinding protein. Journal of Molecular Biology, 134(3), 379-400. doi: 10.1016/0022-2836(79)90359-0. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/55w7j31n
The structure of the gene 5 DNA unwinding protein from bacteriophage fd has been determined by X-ray diffraction analysis of single crystals to 2.3 A resolution using six isomorphous heavy-atom derivatives. The essentially globular monomer appears to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fde05e3e092fdde793d3f0ed4ef6d1e5
http://www.escholarship.org/uc/item/55w7j31n
http://www.escholarship.org/uc/item/55w7j31n
Autor:
Kenneth N. Raymond, Frances A. Jurnak
Publikováno v:
Chemischer Informationsdienst. 5