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Sulfhydryl Reagents (0):
Recent article
Sulfhydryl Reagents
Biochimica et Biophysica Acta (1808)10 2011
Abstract
Replacement of the glycine at position 117 by a cysteine in the melibiose permease creates an interesting phenotype: while the mutant transporter shows still transport activity comparable to the wild type its pre steady-state kinetic properties are drastically altered. The transient charge displaceme...
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PMID: 21801712
PDF is available here.
PDF is available here.
| < More recent | Older article > |
YAKUGAKU ZASSHI (130)10 2010
Abstract
We have employed a combination of cysteine mutagenesis and chemical crosslinking using a photoactivatable sulfhydryl reagent, benzophenone-4-maleimide, to obtain a covalent complex between human galectin-1 and a model glycoprotein ligand, asialofetuin. We previously obtained a crosslinked product wh...
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PMID: 20930491
PDF is available here.
PDF is available here.
Abstract
We examined two such mutations, A40V and G45E, which are positioned near the TM1/E1 boundary and are associated with keratitis ichthyosis deafness (KID) syndrome. Both of these mutants have been reported to form hemichannels that open aberrantly, leading to "leaky" cell membranes. Here, we quantifie...
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PMID: 20584891
PDF is available here.
PDF is available here.
Abstract
We have studied the possible role, in a plant glutamine synthetase (GS), of the different cysteinyl residues present in this enzyme. For this purpose we carried out the site-directed mutagenesis of the cDNA for alpha-GS polypeptide from Phaseolus vulgaris in the positions corresponding to Cys-92, Cy...
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PMID: 20237895
PDF is available here.
PDF is available here.
Abstract
We will describe two methods that use tubulin cysteine reactivity with DTNB in the presence of drug to define ligand-binding characteristics.
Copyright 2010 Elsevier Inc. All rights reserved....
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PMID: 20466146
PDF is available here.
PDF is available here.
Journal of Biological Chemistry (284)30 2009
Abstract
Members of the Acr3 family of arsenite permeases confer resistance to trivalent arsenic by extrusion from cells, with members in every phylogenetic domain. In this study bacterial Acr3 homologues from Alkaliphilus metalliredigens and Corynebacterium glutamicum were cloned and expressed in Escherichia...
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PMID: 19494117
PDF is available here.
PDF is available here.
Abstract
N-ethylmaleimide (NEM) is a sulphydryl blocker which impairs the sulphydryl dependent antioxidant system (mainly glutathione) in the body by alkylating endogenous sulphydryls. This study was designed to investigate the effects of Anzer honey on NEM-induced liver injury in rats. Thirt...
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PMID: 18990552
PDF is available here.
PDF is available here.
Analytical Biochemistry (393)2 2009
Abstract
We report studies on the reactivity of cysteinyl residues of the catalytic domain of PHD2 using an approach in which nondenaturing electrospray ionization-mass spectrometry (ESI-MS) analyses were combined with the use of a thiol library and residue substitution. Among the seven cysteinyl residues of...
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PMID: 19563769
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
We employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of acc...
|
PMID: 19463820
PDF is available here.
PDF is available here.