Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Marita Hiipakka"'
Publikováno v:
Journal of Engineered Fibers and Fabrics, Vol 19 (2024)
Composting offers a potential sustainable end-of-life pathway for nonwoven products that may aerobically disintegrate and eventually biodegrade. Enhancing the biodegradation of nonwovens typically involves incorporating biobased biodegradable fibres.
Externí odkaz:
https://doaj.org/article/d64d71fb1a8d4bacb625363129613a5b
Publikováno v:
Journal of Virology. 75:3034-3037
Here we show that the potential to regulate NFAT is a conserved property of different Nef alleles and that Nef residues involved in membrane targeting and SH3 binding are critical for this function. Cotransfection of an activated protein kinase C-θ
Publikováno v:
Journal of Molecular Biology. 293:1097-1106
The avid binding of HIV-1 Nef to the Src homology-3 (SH3) domain of Hck (KD 250 nM) has been shown to involve an interaction between the RT-loop of Hck-SH3 and residues in Nef outside of its prototypic polyproline type II (PPII) helix-containing SH3-
Autor:
Kalle Saksela, Marika Vähä-Jaakkola, G. Herman Renkema, Iivari Kleino, Jing-Huan Wang, Michael Liss, Satu Kärkkäinen, Marita Hiipakka, Ralf Wagner
Publikováno v:
EMBO reports. 7(2)
We have determined the human genome to contain 296 different Src homology-3 (SH3) domains and cloned them into a phage-display vector. This provided a powerful and unbiased system for simultaneous assaying of the complete human SH3 proteome for the s
Autor:
Marita Hiipakka, Kalle Saksela
Publikováno v:
The Journal of general virology. 83(Pt 12)
The simian immunodeficiency virus (SIV) Nef protein contains a consensus Src-homology 3 (SH3) binding motif. However, no SH3-domain proteins showing strong binding to SIV Nef have yet been found, and its potential capacity for high-affinity SH3 bindi
Publikováno v:
Virology. 286(1)
SH3 domains regulate many normal and pathological cellular processes by guiding specific protein interactions. Studies on binding of HIV-1 Nef to the SH3 domain of the Hck tyrosine kinase have indicated an important role for the SH3 RT-loop region in
Publikováno v:
Virology. 250(2)
HIV-1 Nef has previously been shown to bind to Src homology-3 (SH3) domains of a subset of Src family tyrosine kinases. In addition, Nef has been reported to coprecipitate with a serine/threonine kinase activity termed NAK (for Nef-associated kinase)
Autor:
Marita Hiipakka, Kalle Saksela
Publikováno v:
FEBS Letters. (9):1735-1741
Src-homology (SH3) domain belongs to a class of ubiquitous modular protein domains found in nature. SH3 domains have a conserved surface that recognises proline-rich peptides in ligand proteins, but additional contacts also contribute to binding. Usi