نتایج جستجو برای: cysteine rich metal binding peptide

تعداد نتایج: 896401  

2016
Yu Pan Yanglu Pan Junpeng Zhai Yan Xiong Jinhua Li Xiaobing Du Chenggang Su Xingguo Zhang

We identified a novel member of the metallothionein (MT) family, Cucumis sativus metallothionein-like 2 (CsMTL2), by screening a young cucumber fruit complementary DNA (cDNA) library. The CsMTL2 encodes a putative 77-amino acid Class II MT protein that contains two cysteine (Cys)-rich domains separated by a Cys-free spacer region. We found that CsMTL2 expression was regulated by metal stress an...

Journal: :Proceedings of the National Academy of Sciences 2009

Journal: :Blood 2009
Paul A McEwan Robert K Andrews Jonas Emsley

Platelet glycoprotein Ibalpha (GpIbalpha) interactions with von Willebrand factor (VWF) are a critical early event in platelet adhesion, which contributes to hemostasis and thrombosis. Here we report the structure of a complex between GpIbalpha and a potent peptide inhibitor. The cyclic peptide (CTERMALHNLC) was isolated from a cysteine-constrained phage display library, and in the complex this...

Journal: :Virology 1995
K E Clemens R Brent J Gyuris K Münger

We have used a yeast two-hybrid system to show that human papillomavirus E7 proteins can form oligomeric complexes in vivo. The carboxyl-terminal cysteine-rich metal-binding domain is critical for this activity although amino-terminal sequences also contribute to oligomerization. Our experiments also reveal that E7 possesses an intrinsic transcription activation activity in yeast, which resides...

Journal: :Dalton transactions 2009
Thanh T Ngu Martin J Stillman

Metallothionein are small, cysteine-rich, metal-binding proteins that are found ubiquitously in nature. Most metallothioneins bind multiple metals in two well-defined metal-thiolate clusters. This perspective discusses the use of optical spectroscopy to study the metalation of metallothioneins and the emergence of electrospray ionization mass spectrometry as a means of studying the mechanism of...

2007
Olga Iranzo Chris Cabello Vincent L. Pecoraro

One of the most important chemical concepts is defining how one molecule recognizes and controls the properties of another molecule or ion. Nowhere is this issue more significant than in the field of biomolecular recognition. Metalloproteins efficiently control the geometry and coordination number of metal ions as well as the types of ligands bound to them. Incorporation of metals in the correc...

Journal: :Angewandte Chemie 2007
Olga Iranzo Chris Cabello Vincent L Pecoraro

One of the most important chemical concepts is defining how one molecule recognizes and controls the properties of another molecule or ion. Nowhere is this issue more significant than in the field of biomolecular recognition. Metalloproteins efficiently control the geometry and coordination number of metal ions as well as the types of ligands bound to them. Incorporation of metals in the correc...

Journal: :Plant physiology 1984
P J Jackson E J Roth P R McClure C M Naranjo

Datura innoxia cells from suspension cultures were selected for their ability to grow and divide rapidly in normally lethal concentrations of cadmium. Cells resistant to 12.5, 25, 50, 100, 160, 200, and 250 micromolar cadmium chloride were isolated and utilized to initiate cell suspension cultures resistant to this toxic metal ion. Variant cell lines retained their ability to grow in cadmium af...

Journal: :Molecules 2014
Cillian Byrne Kate M Houlihan Prarthana Devi Paul Jensen Peter J Rutledge

Nitrile hydratase (NHase, EC 4.2.1.84) is a metalloenzyme which catalyses the conversion of nitriles to amides. The high efficiency and broad substrate range of NHase have led to the successful application of this enzyme as a biocatalyst in the industrial syntheses of acrylamide and nicotinamide and in the bioremediation of nitrile waste. Crystal structures of both cobalt(III)- and iron(III)-de...

Journal: :Journal of bacteriology 1992
M V Mendiola Y Jubete F de la Cruz

IS91 is a 1,830-bp insertion sequence that inserts specifically at the sequence CAAG or GAAC of the target and does not duplicate any sequence upon insertion (23). By transposon mutagenesis, we have identified open reading frame 426 (ORF426; bp 454 to 1731) as the putative ORF for the transposase. It displays a cysteine-rich, potential metal-binding domain in its N-terminal region. Adjacent to ...

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