Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Celia Baitinger"'
Publikováno v:
Nucleic Acids Research
Genetic and biochemical studies have previously implicated exonuclease 1 (Exo1) in yeast and mammalian mismatch repair, with results suggesting that function of the protein in the reaction depends on both its hydrolytic activity and its ability to in
Publikováno v:
Proceedings of the National Academy of Sciences. 110:12277-12282
MutLα endonuclease can be activated on covalently continuous DNA that contains a MutSα- or MutSβ-recognizable lesion and a helix perturbation that supports proliferating cell nuclear antigen (PCNA) loading by replication factor C, providing a pote
Publikováno v:
Journal of Biological Chemistry. 278:49505-49511
The roles of ATP binding and hydrolysis by MutS in mismatch repair are poorly understood. MutS E694A, in which Glu-694 of the Walker B motif is substituted with alanine, is defective in hydrolysis of bound ATP and has been reported to support MutL-de
Publikováno v:
Journal of Biological Chemistry. 276:31053-31058
Previous biochemical analysis of Escherichia coli methyl-directed mismatch repair implicates three redundant single-strand DNA-specific exonucleases (RecJ, ExoI, and ExoVII) and at least one additional unknown exonuclease in the excision reaction (Co
Publikováno v:
Proceedings of the National Academy of Sciences. 98:6765-6770
Biochemical studies with model DNA heteroduplexes have implicated RecJ exonuclease, exonuclease VII, exonuclease I, and exonuclease X in Escherichia coli methyl-directed mismatch correction. However, strains deficient in the four exonucleases display
Publikováno v:
Biophysical Journal. 96(3)
Single base mismatches, which represent biosynthetic errors during DNA replication, are corrected by the mismatch repair system (MMR). One of the key players of the MMR reaction in E. coli is MutS, a protein that binds to the mismatch and initiates,
Publikováno v:
The Journal of biological chemistry. 279(27)
We have examined the permissible nucleotide occupancy states of human MutSalpha. The MSH2.MSH6 heterodimer binds 1 mol of ADP and 1 mol of adenosine 5'-O-(thiotriphosphate) (ATPgammaS), with a K(d) for each nucleotide of about 1 microm. Anisotropy me
Publikováno v:
The Journal of neuroscience : the official journal of the Society for Neuroscience. 11(11)
Superprotein is a rapidly axonally transported protein that is conspicuously labeled with 35S-methionine supplied to the cell bodies of retinal ganglion cells. Superprotein candidates are apparent among the rapidly transported proteins of many neuron
Autor:
Celia Baitinger, Mark Willard
Publikováno v:
The Journal of neuroscience : the official journal of the Society for Neuroscience. 7(11)
Synapsin I is a neuronal phosphoprotein that is associated with the cytoplasmic surface of small, clear synaptic vesicles in neuronal synaptic terminals; it may play an important role in synaptic transmission. In vitro, it can interact with fodrin, a
Publikováno v:
Brain research bulletin. 18(6)
Fodrin, a protein related to erythrocyte spectrin, redistributes within the cell in certain situations. We compare such movements of fodrin and several fodrin binding proteins during the processes of axonal transport in neurons, and capping of surfac