نتایج جستجو برای: tlr2tlr4 heterodimer

تعداد نتایج: 5219  

2015
Fangzhong Wang Kuimei Liu Lijuan Han Baojie Jiang Mingyu Wang Xu Fang

The lignocellulose degradation capacity of filamentous fungi has been widely studied because of their cellulase hypersecretion. The p24 proteins in eukaryotes serve important functions in this secretory pathway. However, little is known about the functions of the p24 proteins in filamentous fungi. In this study, four p24 proteins were identified in Penicillium oxalicum. Six p24 double-deletion ...

Journal: :Biochemistry 1999
M E van Brederode I H van Stokkum E Katilius F van Mourik M R Jones R van Grondelle

Energy transfer and the primary charge separation process are studied as a function of excitation wavelength in membrane-bound reaction centers of Rhodobacter sphaeroides in which the excitonically coupled bacteriochlorophyll homodimer is converted to a bacteriochlorophyll-bacteriopheophytin heterodimer, denoted D [Bylina, E. J., and Youvan, D. C. (1988) Proc. Natl. Acad. Sci. U.S. A. 85, 7226]...

2017
Shin Matsubara Akira Shiraishi Tsubasa Sakai Toshimi Okuda Honoo Satake

G protein-coupled receptors (GPCRs) have been found to form heterodimers and modulate or fine-tune the functions of GPCRs. However, the involvement of GPCR heterodimerization and its functional consequences in gonadal tissues, including granulosa cells, have been poorly investigated, mainly due to the lack of efficient method for identification of novel GPCR heterodimers. In this paper, we iden...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2005
Patrick R D'Silva Brenda Schilke William Walter Elizabeth A Craig

Translocation of proteins across the mitochondrial inner membrane is an essential process requiring an import motor having mitochondrial Hsp70 (mtHsp70) at its core. The J protein partner of mtHsp70, Pam18, is an integral part of this motor, serving to stimulate the ATPase activity of mtHsp70. Pam16, an essential protein having an inactive J domain that is unable to stimulate mtHsp70's ATPase a...

Journal: :Frontiers in bioscience : a journal and virtual library 2005
Cui Zhanhua Jacob Gah-Kok Gan Li Lei Venkatarajan Subramanian Mathura Meena Kishore Sakharkar Pandjassarame Kangueane

Protein subunit dimers are either homodimers (consisting of identical polypeptides) or heterodimers (consisting of different polypeptides). Protein dimers are involved in several cellular processes and an understanding of their molecular principle in complexations (subunit-subunit interaction) is essential. This is generally studied using 3D structures of homodimers and heterodimers determined ...

2016
Stijn M Agten Rory R Koenen Hans Ippel Veit Eckardt Philipp von Hundelshausen Kevin H Mayo Christian Weber Tilman M Hackeng

Protein-protein interactions (PPIs) govern most processes in living cells. Current drug development strategies are aimed at disrupting or stabilizing PPIs, which require a thorough understanding of PPI mechanisms. Examples of such PPIs are heteromeric chemokine interactions that are potentially involved in pathological disorders such as cancer, atherosclerosis, and HIV. It remains unclear wheth...

Journal: :Biochemical and biophysical research communications 2013
Manisha Tiwari Shintaro Mikuni Hideki Muto Masataka Kinjo

Two-laser-beam fluorescence cross-correlation spectroscopy (FCCS) is promising technique that provides quantitative information about the interactions of biomolecules. The p50/p65 heterodimer is the most abundant and well understood of the NFκB dimers in most cells. However, the quantitative value of affinity, namely the K(d), for the heterodimer in living cells is not known yet. To quantify th...

Journal: :Cell 2007
Mi Sun Jin Sung Eun Kim Jin Young Heo Mi Eun Lee Ho Min Kim Sang-Gi Paik Hayyoung Lee Jie-Oh Lee

TLR2 in association with TLR1 or TLR6 plays an important role in the innate immune response by recognizing microbial lipoproteins and lipopeptides. Here we present the crystal structures of the human TLR1-TLR2-lipopeptide complex and of the mouse TLR2-lipopeptide complex. Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TL...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1990
L J Ransone J Visvader P Wamsley I M Verma

Jun and Fos nuclear oncoproteins form a complex that regulates transcription from promoters containing activator protein AP-1 binding sites. The leucine-zipper and basic-region domains of both Fos and Jun are necessary for formation of the heterodimer that binds to DNA. Reciprocal mutations in the basic region of Fos or Jun can influence the binding of the heterodimer to DNA, implying a symmetr...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1998
S T Suhr E B Gil M C Senut F H Gage

Our studies of the Bombyx mori ecdysone receptor (BE) revealed that, unlike the Drosophila melanogaster ecdysone receptor (DE), treatment of BE with the ecdysone agonist tebufenozide stimulated high level transactivation in mammalian cells without adding an exogenous heterodimer partner. Gel mobility shift and transfection assays with both the ultraspiracle gene product (Usp) and retinoid X rec...

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