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Institution

Applied Biosystems

About: Applied Biosystems is a based out in . It is known for research contribution in the topics: Mass spectrometry & Capillary electrophoresis. The organization has 1521 authors who have published 1579 publications receiving 285423 citations.


Papers
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Patent
08 Apr 1991
TL;DR: In this paper, a method for achieving desired electroosmotic flow characteristics in a capillary tube having charged surface groups is proposed, where an electrolyte solution containing a compound effective to stably alter the charge of the tube walls is drawn into and through the tube during while the electroosmeotic flow rate in the tube is being monitored.
Abstract: A method for achieving desired electroosmotic flow characteristics in a capillary tube having charged surface groups. An electrolyte solution containing a compound effective to stably alter the charge of the tube walls is drawn into and through the tube during while the electroosmotic flow rate in the tube is being monitored, until a desired electroosmotic flow rate is achieved. The method can be used to optimize electrophoretic separation of charged protein or nucleic acid species in a capillary tube, and to produce capillary tubes with desired charge density properties.

29 citations

Patent
17 Sep 2008
TL;DR: In this article, modification formats having modified nucleotides are provided for siRNA to reduce off-target effects in RNA interference of endogenous genes and further modification formatted siRNAs are demonstrated to be stabilized to nuclease-rich environments.
Abstract: Modification formats having modified nucleotides are provided for siRNA. Short interfering RNA having modification formats and modified nucleotides provided herein reduce off-target effects in RNA interference of endogenous genes. Further modification formatted siRNAs are demonstrated to be stabilized to nuclease-rich environments. Unexpectedly, increasing or maintaining strand bias, while necessary to maintain potency for endogenous RNA interference, is not sufficient for reducing off-target effects in cell biology assays.

29 citations

Journal ArticleDOI
TL;DR: Overall homology between the mammalian and avian enzymes for the 57-amino-acid residue region is 47% and suggests that the two enzymes may share a common evolutionary origin.
Abstract: Medium-chain S-acyl fatty acid synthetase thioester hydrolase (thioesterase II), a discrete monomeric enzyme of 29 kDa, regulates the product specificity of the de novo lipogenic systems in certain specialized mammalian and avian tissues, such as mammary and uropygial glands. The amino acid sequence of a 57-residue region containing the active site of the rat mammary gland enzyme has been established by a combination of amino acid and cDNA sequencing. Thioesterase II was radiolabeled with the serine esterase inhibitor [1,3-14C]diisopropylfluorophosphate and digested sequentially with cyanogen bromide, Staphylococcus aureus V8 protease and trypsin. A radiolabeled tryptic peptide was isolated and sequenced by automated Edman degradation and the location of the active-site residue established. The amino acid sequence was confirmed by sequencing an overlapping, unlabeled peptide, obtained by V8 digestion of the whole enzyme, and by dideoxynucleotide sequencing of a thioesterase II cDNA clone isolated from a λgt11 expression library. The active center contains the motif Gly-Xaa-Ser-Xaa-Gly, characteristic of the serine esterase family of enzymes. A seven-residue region around the essential serine of the rat mammary thioesterase II, Phe-Gly-Met-Ser-Phe-Gly-Ser, is completely homologous with a region of the mallard uropygial thioesterase, recently analyzed by cDNA sequencing, indicating that this is likely to be the active site of the avian enzyme. Overall homology between the mammalian and avian enzymes for the 57-amino-acid residue region is 47% and suggests that the two enzymes may share a common evolutionary origin.

29 citations

Patent
05 Jan 2004
TL;DR: In this article, the authors present a method for the preparation of isotopically enriched N-substituted piperazine acetic acids, which pertains to methods for the extraction of PPIAs.
Abstract: In some embodiments, this invention pertains to isotopically enriched N-substituted piperazine acetic acids. In some embodiments, this invention pertains to methods for the preparation of isotopically enriched N-substituted piperazine acetic acids.

29 citations

Journal ArticleDOI
TL;DR: Although more automation and quality control measures are needed, Pyrosequencing was shown to be a fast and convenient method for determining short stretches of DNA sequence.
Abstract: Pyrosequencing is a relatively recent method for sequencing short stretches of DNA. Because both Pyrosequencing and Sanger dideoxy sequencing were recently used to characterize and validate DNA molecular barcodes in a large yeast gene-deletion project, a meta-analysis of those data allow an excellent and timely opportunity for evaluating Pyrosequencing against the current gold standard, Sanger dideoxy sequencing. Starting with yeast genomic DNA, parallel PCR amplification methods were used to prepared 4747 short barcode-containing constructs from 6000 Saccharomyces cerevisiae gene-deletion strains. Pyrosequencing was optimized for average read lengths of 25-30 bases, which included in each case a 20-mer barcode sequence. Results were compared with sequence data obtained by the standard Sanger dideoxy chain termination method. In most cases, sequences obtained by Pyrosequencing and Sanger dideoxy sequencing were of comparable accuracy, and the overall rate of failure was similar. The DNA in the barcodes is derived from synthetic oligonucleotide sequences that were inserted into yeast-deletion-strain genomic DNA by homologous recombination and represents the most significant amount of DNA from a synthetic source that has been sequenced to date. Although more automation and quality control measures are needed, Pyrosequencing was shown to be a fast and convenient method for determining short stretches of DNA sequence.

29 citations


Authors

Showing all 1521 results

NameH-indexPapersCitations
Richard A. Gibbs172889249708
Friedrich C. Luft113109547619
Alexander N. Glazer7120821068
Vineet Bafna6823642574
Kevin R. Coombes6330823592
Darryl J. Pappin6117029409
Mark D. Johnson6028916103
György Marko-Varga5640912600
Paul Thomas5612844810
Gerald Zon5525611126
Michael W. Hunkapiller5113029756
Bjarni V. Halldorsson5114513180
David H. Hawke501579824
Ellson Y. Chen507128836
Sridhar Hannenhalli4916221959
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
20182
20171
20164
20152
20147
201313