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Kenneth R. Woods

Bio: Kenneth R. Woods is an academic researcher from Cornell University. The author has contributed to research in topics: Amino acid & Peptide sequence. The author has an hindex of 7, co-authored 10 publications receiving 4197 citations. Previous affiliations of Kenneth R. Woods include New York Blood Center & Florida State University.

Papers
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Journal ArticleDOI
TL;DR: The method was developed using 12 proteins for which extensive immunochemical analysis has been carried out and subsequently was used to predict antigenic determinants for the following proteins, finding that the prediction success rate depended on averaging group length.
Abstract: A method is presented for locating protein antigenic determinants by analyzing amino acid sequences in order to find the point of greatest local hydrophilicity. This is accomplished by assigning each amino acid a numerical value (hydrophilicity value) and then repetitively averaging these values along the peptide chain. The point of highest local average hydrophilicity is invariably located in, or immediately adjacent to, an antigenic determinant. It was found that the prediction success rate depended on averaging group length, with hexapeptide averages yielding optimal results. The method was developed using 12 proteins for which extensive immunochemical analysis has been carried out and subsequently was used to predict antigenic determinants for the following proteins: hepatitis B surface antigen, influenza hemagglutinins, fowl plague virus hemagglutinin, human histocompatibility antigen HLA-B7, human interferons, Escherichia coli and cholera enterotoxins, ragweed allergens Ra3 and Ra5, and streptococcal M protein. The hepatitis B surface antigen sequence was synthesized by chemical means and was shown to have antigenic activity by radioimmunoassay.

3,767 citations

Journal ArticleDOI
TL;DR: A computerized method for predicting the locations of protein antigenic determinants is presented, which requires only the amino acid sequence of a protein, and no other information.

327 citations

Journal ArticleDOI
TL;DR: The degree of reduced fragility correlated with the level of DEHP in the cell phase implicating dehylhexylphthalate in PVC containers as the stabilizing agent for red cells.
Abstract: The red blood cells of blood stored in containers made of polyvinylchloride (PVC) film are osmotically more stable and lose on average about 1/3 less hemoglobin than when blood is stored in another plastic [poly-(ethylene-co-ethyl acrylate); EEA]. The stability of uniform volumes of stored red blood cells varies directly with PVC surface area, whereas changes in EEA surface area have comparatively little or no effect. PVC contains high concentrations of the plasticizer, diethylhexylphthalate (DEHP), known to migrate into blood and to have a high potential for toxicity. To determine if DEHP could be the red cell stabilizing agent in PVC, whole blood was stored in containers made from EEA into which was incorporated varying amounts of DEHP. Incorporation of DEHP into EEA significantly reduced erythrocyte osmotic fragility (p = 0.01). The degree of reduced fragility correlated with the level of DEHP in the cell phase implicating DEHP in PVC containers as the stabilizing agent for red cells.

60 citations

Journal ArticleDOI
TL;DR: Proteinoids prepared by thermal copolymerization of 18 common amino acids have been analyzed and the effects of various amino acid reaction mixtures upon the composition of the polymers obtained have been studied.

44 citations


Cited by
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Journal ArticleDOI
22 Oct 1997-Nature
TL;DR: The cloned capsaicin receptor is also activated by increases in temperature in the noxious range, suggesting that it functions as a transducer of painful thermal stimuli in vivo.
Abstract: Capsaicin, the main pungent ingredient in 'hot' chilli peppers, elicits a sensation of burning pain by selectively activating sensory neurons that convey information about noxious stimuli to the central nervous system We have used an expression cloning strategy based on calcium influx to isolate a functional cDNA encoding a capsaicin receptor from sensory neurons This receptor is a non-selective cation channel that is structurally related to members of the TRP family of ion channels The cloned capsaicin receptor is also activated by increases in temperature in the noxious range, suggesting that it functions as a transducer of painful thermal stimuli in vivo

8,186 citations

Journal ArticleDOI
TL;DR: In this article, six monoclonal antibodies have been isolated from mice immunized with synthetic peptide immunogens whose sequences are derived from that of the human c-myc gene product.
Abstract: Six monoclonal antibodies have been isolated from mice immunized with synthetic peptide immunogens whose sequences are derived from that of the human c-myc gene product. Five of these antibodies precipitate p62c-myc from human cells, and three of these five also recognize the mouse c-myc gene product. None of the antibodies sees the chicken p110gag-myc protein. All six antibodies recognize immunoblotted p62c-myc. These reagents also provide the basis for an immunoblotting assay by which to quantitate p62c-myc in cells.

2,520 citations

Journal ArticleDOI
01 Jan 1985-Nature
TL;DR: The complete nucleotide sequence of two human T-cell leukaemia type III (HTLV-III) proviral DNAs each have four long open reading frames, the first two corresponding to the gag and pol genes.
Abstract: The complete nucleotide sequence of two human T-cell leukaemia type III (HTLV-III) proviral DNAs each have four long open reading frames, the first two corresponding to the gag and pol genes. The fourth open reading frame encodes two functional polypeptides, a large precursor of the major envelope glycoprotein and a smaller protein derived from the 3′-terminus long open reading frame analogous to the long open reading frame (lor) product of HTLV-I and -II.

2,358 citations

Journal ArticleDOI
15 May 2001-Proteins
TL;DR: A remarkable improvement in prediction quality has been observed by using the pseudo‐amino acid composition and its mathematical framework and biochemical implication may also have a notable impact on improving the prediction quality of other protein features.
Abstract: The cellular attributes of a protein, such as which compartment of a cell it belongs to and how it is associated with the lipid bilayer of an organelle, are closely correlated with its biological functions. The success of human genome project and the rapid increase in the number of protein sequences entering into data bank have stimulated a challenging frontier: How to develop a fast and accurate method to predict the cellular attributes of a protein based on its amino acid sequence? The existing algorithms for predicting these attributes were all based on the amino acid composition in which no sequence order effect was taken into account. To improve the prediction quality, it is necessary to incorporate such an effect. However, the number of possible patterns for protein sequences is extremely large, which has posed a formidable difficulty for realizing this goal. To deal with such a difficulty, the pseudo-amino acid composition is introduced. It is a combination of a set of discrete sequence correlation factors and the 20 components of the conventional amino acid composition. A remarkable improvement in prediction quality has been observed by using the pseudo-amino acid composition. The success rates of prediction thus obtained are so far the highest for the same classification schemes and same data sets. It has not escaped from our notice that the concept of pseudo-amino acid composition as well as its mathematical framework and biochemical implication may also have a notable impact on improving the prediction quality of other protein features.

1,731 citations

Journal ArticleDOI
20 Jun 1985-Nature
TL;DR: Two distinct but distantly related complementary DNAs encoding proteins sharing human interleukin-1 (IL-1) activity (termed IL-lα and IL-1β), were isolated from a macrophage cDNA library.
Abstract: Two distinct but distantly related complementary DNAs encoding proteins sharing human interleukin-1 (IL-1) activity (termed IL-1 alpha and IL-1 beta), were isolated from a macrophage cDNA library. The primary translation products of the genes are 271 and 269 amino acids long, although expression in Escherichia coli of the carboxy-terminal 159 and 153 amino acids produces IL-1 biological activity.

1,630 citations