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ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities.
The ATP-dependent Clp protease of Escherichia coli consists of two subunits, the ClpP subunit, which has the proteolytic active site, and ClpA, which possesses ATPase activity and activates theExpand
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Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli.
The ATP-dependent Clp protease of Escherichia coli contains two dissimilar components: the Clp A regulatory polypeptide, with two ATP binding sites and intrinsic ATPase activity, and the Clp PExpand
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Clp P represents a unique family of serine proteases.
The amino acid sequence of Clp P, the proteolytic subunit of the ATP-dependent Clp protease of Escherichia coli, closely resembles a protein encoded by chloroplast DNA, which is well conservedExpand
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The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component.
The ATP-binding component (Component II, hereafter referred to as ClpA) of a two-component, ATP-dependent protease from Escherichia coli has been purified to homogeneity. ClpA is a protein withExpand
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The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate.
The clpA gene, which codes for the ATP-binding subunit of the ATP-dependent Clp protease of Escherichia coli, has been sequenced. The coding region contains a single open reading frame for a proteinExpand
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INDIAN SIGN-LANGUAGE.
In 1876 and 1877, Captain W. P. Clark commanded a detachment of Indian scouts-including Pawnees, Shoshones, Arapahoes, Cheyennes, Crows, and Sioux-who conversed in sign language. They made requests,Expand
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Killer cell inhibitory receptors: diversity, specificity, and function
Summary: NK cells selectively kill target cells that fail to express self‐MHC class I molecules. This selective killing results from a balance between inhibitory NK receptors specific for MHC class IExpand
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Organization and sequence of the genes coding for the proton-translocating ATPase of Bacillus megaterium.
We have cloned and sequenced the genes for the subunits of the proton-translocating ATP synthase of Bacillus megaterium QM B1551. The arrangement of the genes is identical to the arrangement of theExpand
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High‐Pressure NiAs‐Type Modification of FeN
Abstract The combination of laser‐heated diamond anvil cells and synchrotron Mössbauer source spectroscopy were used to investigate high‐temperature high‐pressure chemical reactions of iron and ironExpand
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Sequence and Structure of Clp P , the Proteolytic Component of the ATP-dependent Clp Protease of Escherichia COG *
The ATP-dependent Clp protease of Escherichia coli contains two dissimilar components: the Clp A regulatory polypeptide, with two ATP binding sites and intrinsic ATPase activity, and the Clp PExpand
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