Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Scott W. Umlauf"'
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 12:775-778
Novel phenol bis-Mannich adducts were identified as IL-2 expression inhibitors in a T cell proliferation screening assay. Analogues of the lead compound were prepared through parallel synthesis and a highly selective IL-2 inhibitor was discovered tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4115d7a0a2094b4a54f60327fc7fc0a
https://doi.org/10.1016/s0960-894x(02)00011-2
https://doi.org/10.1016/s0960-894x(02)00011-2
Autor:
Sang-Mo Kang, Kurt Brorson, Scott W. Umlauf, Annte-Chen Tran, Bart Beverly, Ronald H. Schwartz
Publikováno v:
Immunological Reviews. 133:177-197
The delivery of costimulation and the effects of the anergic state impinge on IL-2 production via different molecular mechanisms. The strongest experimental support at this stage suggests that CD28 signaling effects mRNA stability of several lymphoki
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e8ec4aa906365290569fd51fea3e78c
https://doi.org/10.1111/j.1600-065x.1993.tb01516.x
https://doi.org/10.1111/j.1600-065x.1993.tb01516.x
Publikováno v:
ChemInform. 33
Novel phenol bis-Mannich adducts were identified as IL-2 expression inhibitors in a T cell proliferation screening assay. Analogues of the lead compound were prepared through parallel synthesis and a highly selective IL-2 inhibitor was discovered tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f68b18f51ab81e8b82f9a0affc1308d7
https://doi.org/10.1002/chin.200225148
https://doi.org/10.1002/chin.200225148
Publikováno v:
Journal of Biological Chemistry. 265:16898-16912
RecA protein aligns homologous single- and double-stranded DNA molecules in three-stranded joints that can extend over thousands of base pairs. When cross-linked by 4‘-amino-4,5‘,8-trimethyl-psoralen the joint structure observed in nonuniform and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5f8e93774a17f2f0c75c4538315c0c19
https://doi.org/10.1016/s0021-9258(17)44847-2
https://doi.org/10.1016/s0021-9258(17)44847-2
Autor:
Scott W. Umlauf, Lendon G. Payne, Ralph P. Braun, Deborah H. Fuller, Lichun Dong, Joel R. Haynes, Mary S. Wu, Arrington Joshua E, Sarah J. Wagner, Michael D. Macklin
Publikováno v:
Journal of virology. 76(9)
Two plasmid vectors encoding the A and B subunits of cholera toxin (CT) and two additional vectors encoding the A and B subunits of theEscherichia coliheat-labile enterotoxin (LT) were evaluated for their ability to serve as genetic adjuvants for par
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::317eaf6f0ba4802c6d5bb73e58f05caa
https://pubmed.ncbi.nlm.nih.gov/11932419
https://pubmed.ncbi.nlm.nih.gov/11932419
Autor:
Scott W. Umlauf, Una S. Ryan
Publikováno v:
Nature Biotechnology. 14:830-830
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::81024d104d1169f85d97bcc9fe34f50f
https://doi.org/10.1038/nbt0796-830
https://doi.org/10.1038/nbt0796-830
Autor:
Scott W. Umlauf, Michael M. Cox
Publikováno v:
The EMBO Journal. 7:1845-1852
A series of sequence changes in the spacer region of the FLP recombination target (FRT) site are presented which drastically reduce site function without affecting recognition by the FLP protein. The effects follow a pattern which indicates that two
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2e132c4ce86b26de2a0aab2881ecf32
https://doi.org/10.1002/j.1460-2075.1988.tb03017.x
https://doi.org/10.1002/j.1460-2075.1988.tb03017.x
Publikováno v:
Molecular and cellular biology. 8(9)
Holliday structures are formed and resolved by FLP protein during site-specific recombination. These structures have been isolated and are visualized in both native and partially denatured states by electron microscopy. No single-strand breaks are fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::846f31cedfc8be0d8e89fb3e9d7fb2ce
https://pubmed.ncbi.nlm.nih.gov/3065624
https://pubmed.ncbi.nlm.nih.gov/3065624