Zobrazeno 1 - 9 of 9 pro vyhledávání: '"E. J. Bures"'
1
Identification of incompletely processed potential carboxypeptidase E substrates from CpEfat/CpEfat mice
Autor: E J, Bures, P L, Courchesne, J, Douglass, K, Chen, M T, Davis, M D, Jones, M D, McGinley, J H, Robinson, C S, Spahr, J, Sun, R C, Wahl, S D, Patterson
Publikováno v: Proteomics. 1(1)
In an attempt to identify peptides that may be involved in the obese phenotype observed in CpEfat/CpEfat mice (deficient in Carboxypeptidase E, CpE) samples from fourteen neuroendocrine tissues in wild-type and CpEfat/CpEfat mice were obtained. Pepti
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::40b9aaef05be28d875d06537227ed467
https://pubmed.ncbi.nlm.nih.gov/11680901
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2
Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry. II. Limitations of complex mixture analyses
Autor: M T, Davis, C S, Spahr, M D, McGinley, J H, Robinson, E J, Bures, J, Beierle, J, Mort, W, Yu, R, Luethy, S D, Patterson
Publikováno v: Proteomics. 1(1)
With an emphasis on obtaining a multitude of high quality tandem mass spectrometry spectra for protein identification, instrumental parameters are described for the liquid chromatography-tandem mass spectrometry analysis of trypsin digested unfractio
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a1d74a36efefda14792c7df83fff800d
https://pubmed.ncbi.nlm.nih.gov/11680890
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3
Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry. I. Profiling an unfractionated tryptic digest
Autor: C S, Spahr, M T, Davis, M D, McGinley, J H, Robinson, E J, Bures, J, Beierle, J, Mort, P L, Courchesne, K, Chen, R C, Wahl, W, Yu, R, Luethy, S D, Patterson
Publikováno v: Proteomics. 1(1)
The proteome of normal male urine from a commercial pooled source has been examined using direct liquid chromatography-tandem mass spectrometry (LC-MS/MS). The entire urinary protein mixture was denatured, reduced and enzymatically digested prior to
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e6496b51f5f86b685adb5fd2378ce7a1
https://pubmed.ncbi.nlm.nih.gov/11680902
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4
Simplification of complex peptide mixtures for proteomic analysis: reversible biotinylation of cysteinyl peptides
Autor: C S, Spahr, S A, Susin, E J, Bures, J H, Robinson, M T, Davis, M D, McGinley, G, Kroemer, S D, Patterson
Publikováno v: Electrophoresis. 21(9)
A rapid means of identifying many components in an enriched mixture of proteins is enzymatic digestion of the entire protein fraction. This complex peptide mixture is then subjected to reversed-phase high performance liquid chromatography (HPLC) coup
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::494bf9c1426c5c81b90b4480f4b45c66
https://pubmed.ncbi.nlm.nih.gov/10870950
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5
A simplified device for protein identification by microcapillary gradient liquid chromatography-tandem mass spectrometry
Autor: M D, McGinley, M T, Davis, J H, Robinson, C S, Spahr, E J, Bures, J, Beierle, J, Mort, S D, Patterson
Publikováno v: Electrophoresis. 21(9)
A simplified device and procedure have been developed for microcapillary gradient liquid chromatography-tandem mass spectrometry (LC-MS/MS). This procedure has proved useful in identifying low level quantities of proteins from sodium dodecyl sulfate-
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8a86153f9f55850a4527340f00aff9a9
https://pubmed.ncbi.nlm.nih.gov/10870954
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6
Human leptin receptor. Determination of disulfide structure and N-glycosylation sites of the extracellular domain
Autor: M, Haniu, T, Arakawa, E J, Bures, Y, Young, J O, Hui, M F, Rohde, A A, Welcher, T, Horan
Publikováno v: The Journal of biological chemistry. 273(44)
The leptin receptor (OB-R) is a member of the class I cytokine receptor family and mediates the weight regulatory effects of its ligand through interaction with cytoplasmic kinases. The extracellular domain of this receptor is comprised of two immuno
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9304d3d44a6fbe494adae01b1465b275
https://pubmed.ncbi.nlm.nih.gov/9786864
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7
Interactions between brain-derived neurotrophic factor and the TRKB receptor. Identification of two ligand binding domains in soluble TRKB by affinity separation and chemical cross-linking
Autor: M, Haniu, S, Montestruque, E J, Bures, J, Talvenheimo, R, Toso, S, Lewis-Sandy, A A, Welcher, M F, Rohde
Publikováno v: The Journal of biological chemistry. 272(40)
The extracellular domain of the human neurotrophin TRKB receptor expressed in Chinese hamster ovary cells is a highly glycosylated protein, possessing binding ability for brain-derived neurotrophic factor (BDNF). Two distinct ligand binding domains o
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8151695a077ec884d4a35270a9766a40
https://pubmed.ncbi.nlm.nih.gov/9312147
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8
Design, synthesis, and characterization of a protein sequencing reagent yielding amino acid derivatives with enhanced detectability by mass spectrometry
Autor: R, Aebersold, E J, Bures, M, Namchuk, M H, Goghari, B, Shushan, T C, Covey
Publikováno v: Protein science : a publication of the Protein Society. 1(4)
We report the design, chemical synthesis, and structural and functional characterization of a novel reagent for protein sequence analysis by the Edman degradation, yielding amino acid derivatives rapidly detectable at high sensitivity by ion-evaporat
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6f0b6016fb7a590d1ddf20db1aed9960
https://pubmed.ncbi.nlm.nih.gov/1304351
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