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Title: Phosphoprotein binding agents and methods of their use

Patent ·
OSTI ID:1175129
; ; ;

The invention provides reagents and methods for characterizing (i.e., identification and/or quantitation) the phosphorylation states of proteins. Proteins may be post-transcriptionally modified such that they contain phosphate groups at either some or all of their serine, threonine, tyrosine, histidine, and/or lysine amino acid residues. In many cases the extent to which a protein is phosphorylated determines it bioactivity, i.e., its ability to effect cell functions such as differentiation, division, and metabolism. Hence, a powerful tool for diagnosing various diseases and for furthering the understanding of protein--protein interactions is provided.

Research Organization:
Pacific Northwest National Laboratory (PNNL), Richland, WA (United States)
Sponsoring Organization:
USDOE
DOE Contract Number:
AC06-76RL01830
Assignee:
Battelle Memorial Institute (Richland, WA)
Patent Number(s):
6,818,454
Application Number:
09/788,286
OSTI ID:
1175129
Country of Publication:
United States
Language:
English

References (11)

Quantitative and Selective Fluorophore Labeling of Phosphoserine on Peptides and Proteins: Characterization at the Attomole Level by Capillary Electrophoresis and Laser-Induced Fluorescence journal February 1995
Utilizing the Peptidyl-Prolyl Cis-Trans Isomerase Pin1 as a Probe of Its Phosphorylated Target Proteins: Examples of Binding to Nuclear Proteins in a Human Kidney Cell Line and to Tau in Alzheimer's Diseased Brain journal January 2001
Studies on the Methods for the Determination of Phosphorylation Sites in Highly Phosphorylated Peptides or Proteins: Phosphorylation Sites of Hen Egg White Riboflavin Binding Protein journal October 1986
Expression and phosphorylation status of retinoblastoma protein in adult T-cell leukemia/lymphoma journal April 2000
Sequence analysis of phosphoserine-containing peptides: Modification for picomolar sensitivity journal August 1986
Quantification of tau phosphorylated at threonine 181 in human cerebrospinal fluid: a sandwich ELISA with a synthetic phosphopeptide for standardization journal May 2000
Chemical modification of phosvitin: Preparation of dimethylaminovitin and methylmercaptovitin and their utility for elucidation of phosvitin primary structure journal January 1980
Comparative quantification and identification of phosphoproteins using stable isotope labeling and liquid chromatography/mass spectrometry journal January 2000
Selective analysis of phosphopeptides within a protein mixture by chemical modification, reversible biotinylation and mass spectrometry journal January 2001
Quantitative analysis of complex protein mixtures using isotope-coded affinity tags journal October 1999
Characterization of Serine and Threonine Phosphorylation Sites in β-Elimination/Ethanethiol Addition-Modified Proteins by Electrospray Tandem Mass Spectrometry and Database Searching journal October 1998

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