K
Kevin J. Barringer
Researcher at Salk Institute for Biological Studies
Publications - 8
Citations - 2413
Kevin J. Barringer is an academic researcher from Salk Institute for Biological Studies. The author has contributed to research in topics: Pichia pastoris & Gene. The author has an hindex of 7, co-authored 8 publications receiving 2343 citations.
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Isothermal, in vitro amplification of nucleic acids by a multienzyme reaction modeled after retroviral replication.
John C. Guatelli,Kristina Marie Whitfield,Deborah Y. Kwoh,Kevin J. Barringer,Douglas D. Richman,Thomas R. Gingeras +5 more
TL;DR: A target nucleic acid sequence can be replicated exponentially in vitro under isothermal conditions by using three enzymatic activities essential to retroviral replication: reverse transcriptase, RNase H, and a DNA-dependent RNA polymerase, and this reaction accumulates cDNA and RNA copies of the original target.
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Pichia pastoris as a host system for transformations.
TL;DR: A methylotrophic yeast, Pichia pastoris, is developed as a host for DNA transformations based on an auxotrophic mutant host of P. pastoris which is defective in histidinol dehydrogenase.
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Functional characterization of the two alcohol oxidase genes from the yeast Pichia pastoris.
TL;DR: In Pichia pastoris, alcohol oxidase is the first enzyme in the methanol utilization pathway and is encoded by two genes, AOX1 and AOX2, which appear to be regulated in the same manner.
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Structural comparison of the Pichia pastoris alcohol oxidase genes
Patricia J Koutz,Geneva Ruth Davis,Cathy A. Stillman,Kevin J. Barringer,James M. Cregg,Gregory Patrick Thill +5 more
TL;DR: Although alcohol oxidase is found in peroxisomes of P. pastoris, the AOX amino acid sequences did not contain a peptide sequence similar to the peroxISomal transport sequence found at the C‐terminus of somePeroxisomally located proteins in higher eukaryotes.
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Blunt-end and single-strand ligations by Escherichia coli ligase: influence on an in vitro amplication scheme
TL;DR: The results of this study indicate that E. coli ligase also joins blunt-ended DNA molecules and some single-stranded oligodeoxyribonucleotides, in the absence of a complementary template, with an efficiency which is sensitive to both the concentrations of DNA substrate and enzyme.