Výsledky vyhledávání - "Kenneth H. Aoki"

Asn to Lys mutations at three sites which are N-glycosylated in the mammalian protein decrease the aggregation of Escherichia coli-derived erythropoietin

Autor: Thomas C. Boone, Linda O. Narhi, Steve Elliott, Janet Cheetham, Kenneth H. Aoki, Tsutomu Arakawa, Jie Wen

Publikováno v: Protein Engineering, Design and Selection. 14:135-140

Erythropoietin (EPO) derived from Escherichia coli is unstable to elevated temperature and tends to aggregate with time, making it unsuitable for high-resolution structure analysis. The mammalian EPO contains about 40% carbohydrate, which makes this

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d02e89d73fde3f32b75804f2228c712
https://doi.org/10.1093/protein/14.2.135

Zobrazit plný text záznamu

Changes in Conformation and Stability upon Formation of Complexes of Erythropoietin (EPO) and Soluble EPO Receptor

Autor: John S. Philo, Linda O. Narhi, Tsutomu Arakawa, Kenneth H. Aoki

Publikováno v: Journal of Protein Chemistry. 16:213-225

Erythropoietin (EPO) is a glycoprotein hormone which belongs to the four-helical-bundle cytokine family and regulates the level of circulating red blood cells. The EPO receptor (EPOR) belongs to the cytokine-receptor family of proteins. While many of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46f0d920b67759abb24cb21ccf2fe434
https://doi.org/10.1023/a:1026330909461

Zobrazit plný text záznamu

The effect of carbohydrate on the structure and stability of erythropoietin

Autor: Thomas W. Strickland, Linda O. Narhi, Michael F. Rohde, Tsutomu Arakawa, Tom Boone, Kenneth H. Aoki, R Elmore

Publikováno v: Journal of Biological Chemistry. 266:23022-23026

Erythropoietin is a glycoprotein hormone that stimulates the maturation of late erythroid progenitor cells. It has three N-linked and one O-linked carbohydrates which play an important role in the biosynthesis and biological activities of the protein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3d6a4fbde81e71b7e0ed1cfbd3a1d93f
https://doi.org/10.1016/s0021-9258(18)54457-4

Zobrazit plný text záznamu

Differentiation of the local structure around tryptophan 51 and 64 in recombinant human erythropoietin by tryptophan phosphorescence

Autor: Bruce A. Kerwin, Kenneth H. Aoki, Giovanni B. Strambini, Margherita Gonelli

Publikováno v: Photochemistry and photobiology 84 (2008): 1172–1181. doi:10.1111/j.1751-1097.2008.00307.x
info:cnr-pdr/source/autori:Kerwin BA, Aoki KH, Gonelli M, Strambini GB./titolo:Differentiation of the Local Structure Around Tryptophan 51 and 64 in Recombinant Human Erythropoietin by Tryptophan Phosphorescence./doi:10.1111%2Fj.1751-1097.2008.00307.x/rivista:Photochemistry and photobiology/anno:2008/pagina_da:1172/pagina_a:1181/intervallo_pagine:1172–1181/volume:84

Recombinant human erythropoietin is a 4-helix bundle, glycosylated cytokine containing three tryptophan residues at positions 51, 64 and 88 whose phosphorescence emission may represent a sensitive probe of the structure at multiple sites near or at t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b36b97ba3cee2ee3548eb6010ba34e0
https://pubmed.ncbi.nlm.nih.gov/18331401

Zobrazit plný text záznamu

Biophysical comparability of the same protein from different manufacturers: a case study using Epoetin alfa from Epogen and Eprex

Autor: Sungae S. Park, Bruce A. Kerwin, Kenneth H. Aoki, Songpon Deechongkit

Publikováno v: Journal of pharmaceutical sciences. 95(9)

This study focuses on the development and application of biophysical methodology to characterize conformations of Epogen and Eprex, the injectable formulations of recombinant human Epoetin alfa produced by different manufacturers and commonly used fo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::714af94d6acdc67f2c2b9052e2533b92
https://pubmed.ncbi.nlm.nih.gov/17721976

Zobrazit plný text záznamu

Copper staining method for extracting biologically active proteins from native gels

Autor: Tsutomu Arakawa, Kenneth H. Aoki, Elizabeth A. Mendiaz, Jette Wypych, Mei Zhang, Keith Langley, Tiansheng Li, John S. Philo, Tom Horan, Moeka Kuwamoto, Yoshiko Kita, Jie Wen

Publikováno v: Bioscience, biotechnology, and biochemistry. 65(6)

An attempt was made to make protein bands visible on native gel using copper staining, since such a mild staining procedure would make the entire native gel electrophoresis process non-denaturing. Copper staining not only was able to detect various p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36188c4c4ab79b3498eaf29978058804
https://pubmed.ncbi.nlm.nih.gov/11471730

Zobrazit plný text záznamu

Stabilization of human recombinant erythropoietin through interactions with the highly branched N-glycans

Autor: Tsutomu Arakawa, Tomokazu Itai, Teruko Toyoda, Haruki Yamaguchi, Kenneth H. Aoki

Publikováno v: Journal of biochemistry. 128(5)

Human erythropoietin (EPO) produced in Chinese hamster ovary cells (CHO-EPO) is a hydrophobic protein stabilized by the highly branched complex-type N-glycans. To characterize the stabilizing effect of the N-glycans, the properties of enzymatically N

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2465d5a8031d8e6167db82bf99ab6daf
https://pubmed.ncbi.nlm.nih.gov/11056384

Zobrazit plný text záznamu

Engineering a soluble extracellular erythropoietin receptor (EPObp) in Pichia pastoris to eliminate microheterogeneity, and its complex with erythropoietin

Publikováno v: Protein engineering. 12(6)

4 To whom correspondence should be addressed The extracellular ligand-binding domain (EPObp) of the human EPO receptor (EPOR) was expressed both in CHO (Chinese Hamster Ovary) cells and in Pichia pastoris. The CHO and yeast expressed receptors showed

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87e075ae637e1734e4dadf9bfc5f1a80
https://pubmed.ncbi.nlm.nih.gov/10388848

Zobrazit plný text záznamu

NMR structure of human erythropoietin and a comparison with its receptor bound conformation

Autor: Rashid Syed, Thomas J. Hoeffel, Joan C. Egrie, Duncan M. Smith, Timothy S. Harvey, Janet Cheetham, Kenneth H. Aoki, Janice L. Stevenson

Publikováno v: Nature structural biology. 5(10)

The solution structure of human erythropoietin (EPO) has been determined by nuclear magnetic resonance spectroscopy and the overall topology of the protein is revealed as a novel combination of features taken from both the long-chain and short-chain

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e05cbe16010d52eb27cb42dde05fcb67
https://pubmed.ncbi.nlm.nih.gov/9783743

Zobrazit plný text záznamu

Efficiency of signalling through cytokine receptors depends critically on receptor orientation

Autor: Janet Finer-Moore, David J. Matthews, Rashid Syed, Jiandong Zhang, Joan C. Egrie, John J. Wendoloski, Karen C. Sitney, Bradley A. Katz, Scott W. Reid, Arthur J. Chirino, Osslund Timothy D, Cuiwei Li, Robert M. Stroud, Hangjun Zhan, Steven G. Elliott, Janet Cheetham, Kenneth H. Aoki, Beishan Liu

Publikováno v: Nature. 395(6701)

Human erythropoietin is a haematopoietic cytokine required for the differentiation and proliferation of precursor cells into red blood cells. It activates cells by binding and orientating two cell-surface erythropoietin receptors (EPORs) which trigge

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fbfbe1134944f581e788d1d733855d6
https://pubmed.ncbi.nlm.nih.gov/9774108

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání