IPC분류정보
국가/구분 |
United States(US) Patent
등록
|
국제특허분류(IPC7판) |
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출원번호 |
US-0349040
(1999-07-07)
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발명자
/ 주소 |
- Manoharan, Muthiah
- Cook, Phillip Dan
- Prakash, Thazha P.
- Mohan, Venkatraman
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출원인 / 주소 |
- ISIS Pharmaceuticals, Inc.
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대리인 / 주소 |
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인용정보 |
피인용 횟수 :
13 인용 특허 :
72 |
초록
▼
The present invention provides oligomers which are specifically hybridizable with a selected sequence of RNA or DNA wherein at least one of the nucleoside moieties of the oligomer is modified to include a guanidinium group. These oligomers are useful for diagnostic, therapeutic and investigative pur
The present invention provides oligomers which are specifically hybridizable with a selected sequence of RNA or DNA wherein at least one of the nucleoside moieties of the oligomer is modified to include a guanidinium group. These oligomers are useful for diagnostic, therapeutic and investigative purposes.
대표청구항
▼
The present invention provides oligomers which are specifically hybridizable with a selected sequence of RNA or DNA wherein at least one of the nucleoside moieties of the oligomer is modified to include a guanidinium group. These oligomers are useful for diagnostic, therapeutic and investigative pur
The present invention provides oligomers which are specifically hybridizable with a selected sequence of RNA or DNA wherein at least one of the nucleoside moieties of the oligomer is modified to include a guanidinium group. These oligomers are useful for diagnostic, therapeutic and investigative purposes. dase Assay, Anal. Biochem. 118:173-184 (1981). Doughty and Gruenstein, Chloride -insensitive, glycine-phenylalanine-naphthylamide hydrolysis at neutral pH in human skin fibroblasts, Biochem. and Cell Biol. 64:772 (1986). Ikehara et al., Dipeptidyl-peptidase IV from Rat Liver, Meth. Enzymol. 244:215-227 (1994). Jadot et al., Intralysosomal hydrolysis of glycyl-L-phenylalanine 2-naphthylamide, Biochem. J. 219:965-970 (1984). Klinkenberg, A Dominant Negative Mutation in Saccharomyces cerevisiae Methionine Aminopeptidase-1 Affects Catalysis and Interferes with the Function of Methionine Aminopeptidase-2, Archives of Biochemistry and Biophysics, vol. 347, No. 2, pp. 193-200 (1997). Larrabee et al., High-Pressure Liquid Chromatographic Method for the Assay of Methionine Aminopeptidase Activity: Application to the Study of Enzymatic Inactivation, Anal. Biochem. 269:194-198 (1999). Lin, Purification and Characterization of an Enzyme Hydrolyzing L-Methionine-4-Nitroanilide From Germinated Sweet Potato Roots, Bot Bull Acad Sin, vol. 35, pp. 25-32 (1994). Liu et al., Structure of Human Methionine Aminopeptidase-2 Complexed with Fumagillin, Science 282:1324-1327 (1998). Lowther et al., The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase, Proc. Natl. Acad. Sci. USA 95:12153-12157 (1998). Moerschell et al., The Specificities of Yeast Methionine Aminopeptidase and Acetylation of Amino-terminal Methionine in Vivo, J. Biol. Chem. 265:19638-19643 (1990). Moore et al., Chromatography of Amino Acids on Sulfonated Polystyrene Resins, Anal. Biochem. 30:1185-1190 (1958). Proost et al., Truncation of Macrophage-derived Chemokine by CD26/Dipeptidyl-Peptidase IV beyond Its Predicted Cleavage Site Affects Chemotactic Activity and CC Chemokine Receptor 4 Interaction, J. Biol. Chem. 274:3988-3993 (1999). Roth, Fluorescence Reaction for Amino Acids, Anal. Chem. 43:880-882 (1971). Stein et al., Amino Acid Analysis with Fluorescamine at the Picomole Level, Arch. Biochem. Biophys. 155:202-212 (1973). Tsunasawa et al., Amino-terminal Processing of Mutant forms of Yeast Iso-1-cytochrome c, J. Biol. Chem. 260:5382-5391 (1985). Walker et al., Yeast (Saccharomyces cerevisiae) methionine aminopeptidase I: rapid purification and improved activity assay, Biotechnol. Appl. Biochem. 29:157-163 (1999). Zuo et al., A Protease Assay via Precolumn Derivatization and High-Performance Liquid Chromatography, Anal. Biochem. 222:514-516 (1994).
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