Zobrazeno 1 - 10
of 80
pro vyhledávání: '"F, Nore"'
Autor:
Noriko Hamada-Kawaguchi, Beston F. Nore, Rula Zain, Ylva Engström, C. I. Edvard Smith, Daisuke Yamamoto
Publikováno v:
Frontiers in Bioscience-Landmark, Vol 28, Iss 6, p 124 (2023)
Background: Bruton’s tyrosine kinase (BTK) is a non-receptor type tyrosine kinase originally identified as the genetic signature responsible for X-linked agammaglobulinemia (XLA) when mutated. Its functional form is required for B lymphocyte matura
Externí odkaz:
https://doaj.org/article/43bb95b004f24c748b0d467d9b16ba40
Publikováno v:
The Iraqi Journal of Agricultural science, Vol 52, Iss 2 (2021)
This study was aimed to investigate the Open Reading Frame-112 (ORF-112) gene, which encoded for a hypothetical 218 amino acids protein in Streptomyces bacteria. A complete ORF-112 gene was synthesized, with addition of a 6xHis-Tag at the N-terminal
Externí odkaz:
https://doaj.org/article/3832b2143c444a08aef0cd9350a05041
Publikováno v:
Diyala Journal of Medicine, Vol 14, Iss 1 (2018)
Background:Hepatitis C virus is a common cause of liver disease, hepatitis C virus exhibits high degree of genetic heterogeneity with characterized regional variations in genotype prevalence. Objective: To determine the prevalence of HCV genotypes
Externí odkaz:
https://doaj.org/article/2d225af4a6ba47049a00e386720d4a46
Autor:
Manuela O Gustafsson, Dara K Mohammad, Erkko Ylösmäki, Hyunseok Choi, Subhash Shrestha, Qing Wang, Beston F Nore, Kalle Saksela, C I Edvard Smith
Publikováno v:
PLoS ONE, Vol 12, Iss 4, p e0174909 (2017)
Bruton's Tyrosine Kinase (BTK) is a cytoplasmic protein tyrosine kinase with a fundamental role in B-lymphocyte development and activation. The nucleocytoplasmic shuttling of BTK is specifically modulated by the Ankyrin Repeat Domain 54 (ANKRD54) pro
Externí odkaz:
https://doaj.org/article/bce0773e704f4ae98bda97980d431bb9
Publikováno v:
PLoS ONE, Vol 11, Iss 8, p e0160255 (2016)
Protein kinase B (AKT) phosphorylates numerous substrates on the consensus motif RXRXXpS/T, a docking site for 14-3-3 interactions. To identify novel AKT-induced phosphorylation events following B cell receptor (BCR) activation, we performed proteomi
Externí odkaz:
https://doaj.org/article/0c343840666a45c185a4c852de340ad4
Autor:
Sirwan S. Sleman, Hani N. Hermiz, Shahla M.S. Kirkuki, Beston F. Nore, Rana M. Al-Obaidi, Questan A. Ameen, Ahmed Sami Shaker, Sehand K. Arif, Taher R. Al-Khatib
Publikováno v:
مجلة الانبار للعلوم البيطرية, Vol 13, Iss 2, Pp 100-108 (2020)
The current study conducted to detect the genetic diversity between four genetic groups of Kurdish local chicken using RAPD-PCR technique. Ten random markers used to amplified DNA were selected for genotyping the four lines. One hundred twenty four p
Publikováno v:
Journal of Sulaimani Medical College. 9:409-419
Publikováno v:
The Iraqi Journal of Agricultural science, Vol 52, Iss 2 (2021)
This study was aimed to investigate the Open Reading Frame-112 (ORF-112) gene, which encoded for a hypothetical 218 amino acids protein in Streptomyces bacteria. A complete ORF-112 gene was synthesized, with addition of a 6xHis-Tag at the N-terminal
Translocation-generated ITK-FER and ITK-SYK fusions induce STAT3 phosphorylation and CD69 expression
Autor:
C. I. Edvard Smith, Dara K. Mohammad, Samir El Andaloussi, Rula Zain, Narmeen N. Fathi, André Görgens, Beston F. Nore
Publikováno v:
Biochemical and Biophysical Research Communications. 504:749-752
Many cancer types carry mutations in protein tyrosine kinase (PTK) and such alterations frequently drive tumor progression. One category is gene translocation of PTKs yielding chimeric proteins with transforming capacity. In this study, we characteri
Autor:
C. I. Edvard Smith, Dara K. Mohammad, Abdalla J. Mohamed, Manuela O. Gustafsson, Beston F. Nore
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 78:63-74
The Protein kinase B (AKT) regulates a plethora of intracellular signaling proteins to fine-tune signaling of multiple pathways. Here, we found that following B-cell receptor (BCR)-induced tyrosine phosphorylation of the cytoplasmic tyrosine kinase S