Zobrazeno 1 - 10
of 13
pro vyhledávání: '"J R Casas-Finet"'
Autor:
Samuel H. Wilson, C J Luneau, B M Merrill, Kenneth R. Williams, Aseem Kumar, Richard L. Karpel, J R Casas-Finet
Publikováno v:
Journal of Biological Chemistry. 265:17094-17100
A1 is a core protein of the eukaryotic heterogeneous nuclear ribonucleoprotein complex and is under study here as a prototype single-stranded nucleic acid-binding protein. A1 is a two-domain protein, NH2-terminal and COOH-terminal, with highly conser
Publikováno v:
Developments in biologicals. 122
In this paper, the steps required to validate a liquid chromatography peptide mapping method with mass spectrometric detection (LC-MS) for use as an identity test and characterization tool are presented. All aspects of peptide mapping are evaluated a
Publikováno v:
Photochemistry and photobiology. 70(4)
Bisimidazoacridones (BIA) are highly selective antineoplastic and antiviral agents. Ultraviolet-visible spectroscopy and steady-state and time-resolved fluorescence spectroscopy studies were carried out to probe the behavior of BIA in aqueous and non
Publikováno v:
Journal of molecular biology. 287(1)
HIV-1 nucleocapsid protein (NCp7) is a double zinc-fingered protein that has been traditionally implicated in viral RNA recognition and packaging, in addition to its tight association with genomic RNA and tRNA primer within the virion nucleocapsid. T
Publikováno v:
Journal of molecular biology. 285(1)
The three-dimensional solution structure of circulin A, a 30 residue polypeptide from the African plant Chassalia parvifolia, has been determined using two-dimensional 1H-NMR spectroscopy. Circulin A was originally identified based upon its inhibitio
Autor:
R, Goel, W A, Beard, A, Kumar, J R, Casas-Finet, M P, Strub, S J, Stahl, M S, Lewis, K, Bebenek, S P, Becerra, T A, Kunkel
Publikováno v:
Biochemistry. 32(48)
Virion-derived HIV-1 reverse transcriptase (RT) has subunits of molecular mass 66 and 51 kDa (p66 and p51, respectively) in an approximately 1:1 ratio. Since enzyme activity appears to depend on dimerization of these subunits, identification of criti
Publikováno v:
The Journal of biological chemistry. 268(30)
Rat DNA polymerase beta (beta-pol) is a 39-kDa monomeric protein, organized in two structurally and functionally distinct domains. The 8-kDa NH2-terminal domain binds single-stranded (ss) DNA, whereas the 31-kDa COOH-terminal domain does not. To faci
Publikováno v:
Journal of molecular biology. 229(4)
With a view toward further understanding the structure-function relationships of the eukaryotic heterogeneous ribonucleoprotein (hnRNP) A1, and in particular its multiplicity of nucleic acid-interactive domains, we have studied the nucleic acid bindi
Publikováno v:
The Journal of biological chemistry. 266(29)
The 8- and 31-kDa fragments of beta-polymerase, prepared by controlled proteolysis as described (Kumar, A., Widen, S. G., Williams, K. R., Kedar, P., Karpel, R. L., and Wilson, S. H. (1990) J. Biol. Chem. 265, 2124-2131), constitute domains that are
Autor:
A, Kumar, J R, Casas-Finet, C J, Luneau, R L, Karpel, B M, Merrill, K R, Williams, S H, Wilson
Publikováno v:
The Journal of biological chemistry. 265(28)
A1 is a core protein of the eukaryotic heterogeneous nuclear ribonucleoprotein complex and is under study here as a prototype single-stranded nucleic acid-binding protein. A1 is a two-domain protein, NH2-terminal and COOH-terminal, with highly conser