نتایج جستجو برای: dimerization

تعداد نتایج: 10337  

Journal: :ACS Catalysis 2021

The selective dimerization of CO2 into glycolaldehyde is achieved in a one-pot two-step process via formaldehyde as key intermediate. first step concerns the iron-catalyzed reductio...

Journal: :Proteins 2016
Fabiana Malaga Ory Mayberry David J Park Michael E Rodgers Dmitri Toptygin Robert F Schleif

Genetic experiments with full length AraC and biophysical experiments with its dimerization domain plus linker suggest that arabinose binding to the dimerization domain changes the properties of the inter-domain linker which connects the dimerization domain to the DNA binding domain via interactions that do not depend on the DNA binding domain. Normal AraC function was found to tolerate conside...

2014
Yingzhi Xu He Li Ying-Hua Jin Jun Fan Fei Sun

3-Hydroxyacyl-CoA dehydrogenase (HAD, EC 1.1.1.35) is a homodimeric enzyme localized in the mitochondrial matrix, which catalyzes the third step in fatty acid β-oxidation. The crystal structures of human HAD and subsequent complexes with cofactor/substrate enabled better understanding of HAD catalytic mechanism. However, numerous human diseases were found related to mutations at HAD dimerizatio...

Journal: :Organometallics 2010
Do W Lee Chae S Yi

The cationic ruthenium-hydride complex [(eta(6)-C(6)H(6))(PCy(3))(CO)RuH](+)BF(4) (-) was found to be a highly regioselective catalyst for the ethylene dimerization reaction to give 2-butene products (TOF = 1910 h(-1), >95% selectivity for 2-butenes). The dimerization of styrene exclusively produced the head-to-tail dimer (E)-PhCH(CH(3))CH=CHPh at an initial turnover rate of 2300 h(-1). A rapid...

Journal: :Molecular biology of the cell 2008
Lise Roth Cécile Nasarre Sylvie Dirrig-Grosch Dominique Aunis Gérard Crémel Pierre Hubert Dominique Bagnard

Neuropilin-1 (NRP1) is a transmembrane receptor playing a pivotal role in the control of semaphorins and VEGF signaling pathways. The exact mechanism controlling semaphorin receptor complex formation is unknown. A structural analysis and modeling of NRP1 revealed a putative dimerization GxxxG motif potentially important for NRP1 dimerization and oligomerization. Our data show that this motif me...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1997
D Krylov K Kasai D R Echlin E J Taparowsky H Arnheiter C Vinson

We describe a method to design dominant-negative proteins (D-N) to the basic helix-loop-helix-leucine zipper (B-HLHZip) family of sequence-specific DNA binding transcription factors. The D-Ns specifically heterodimerize with the B-HLHZip dimerization domain of the transcription factors and abolish DNA binding in an equimolar competition. Thermal denaturation studies indicate that a heterodimer ...

Journal: :Glycobiology 1998
B J van Klinken A W Einerhand H A Büller J Dekker

Mucins are synthesized and secreted by many epithelia. They are complex glycoproteins that offer cytoprotection. In their functional configuration, mucins form oligomers by a biosynthetic process that is poorly understood. A family of four human gastrointestinal mucin genes (MUC2, MUC5AC, MUC5B, and MUC6) is clustered to chromosome 11p15.5. To study oligomerization of these related mucins, we p...

Journal: :PloS one 2015
Bo-Lin Ho Shu-Chun Cheng Lin Shi Ting-Yun Wang Kuan-I Ho Chi-Yuan Chou

BACKGROUND A highly pathogenic human coronavirus (CoV), Middle East respiratory syndrome coronavirus (MERS-CoV), has emerged in Jeddah and other places in Saudi Arabia, and has quickly spread to European and Asian countries since September 2012. Up to the 1st October 2015 it has infected at least 1593 people with a global fatality rate of about 35%. Studies to understand the virus are necessary...

Journal: :The Journal of biological chemistry 2001
F Zhang P R Romano T Nagamura-Inoue B Tian T E Dever M B Mathews K Ozato A G Hinnebusch

Protein kinase PKR is activated by double-stranded RNA (dsRNA) and phosphorylates translation initiation factor 2alpha to inhibit protein synthesis in virus-infected mammalian cells. PKR contains two dsRNA binding motifs (DRBMs I and II) required for activation by dsRNA. There is strong evidence that PKR activation requires dimerization, but the role of dsRNA in dimer formation is controversial...

Journal: :American journal of physiology. Lung cellular and molecular physiology 2014
Dhara Patel Sharath Kandhi Melissa Kelly Boon Hwa Neo Michael S Wolin

The activity of glucose-6-phosphate dehydrogenase (G6PD) controls a vascular smooth muscle relaxing mechanism promoted by the oxidation of cytosolic NADPH, which has been associated with activation of the 1α form of protein kinase G (PKG-1α) by a thiol oxidation-elicited subunit dimerization. This PKG-1α-activation mechanism appears to contribute to responses of isolated endothelium-removed bov...

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