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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Chlorpropamide, carbamazepine and clofibrate have an antidiuretic action in patients with neurohypophyseal diabetes insipidus which is qualitatively similar to that of antidiuretic hormone (ADH). 2. An additive antidiuretic effect is produced by combination of chlorpropamide and carbamazepine with small dosages of ADH. 3. After an immediate and transient antidiuresis, a single intravenous bolus injection of lysine vasopressin given during treatment with chlorpropamide, chlorpropamide with a continuous intravenous infusion of lysine vasopressin, carbamazepine or clofibrate, resulted in increased water diuresis for 12-24 h or longer. 4. This paradoxical diuresis was not observed during treatment with chlorothiazide. 5. It is suggested that the antidiuretic action of chlorpropamide, carbamazepine and clofibrate is localized at the receptor site for ADH in the distal renal tubular cell.
Clin Sci Mol Med 1975 Oct
PMID:Paradoxical diuresis after vasopressin administration to patients with neurohypophyseal diabetes insipidus treated with chlorpropamide, carbamazepine or clofibrate. 119 87

1. Five healthy male subjects were studied by continuous infusion of L-[alpha-15N]lysine over 20-30 h with timed blood and urine samples, and two or three percutaneous needle biopsies of vastus lateralis muscle. 2. A standard creatine-free diet, quantitatively related to body surface area, was given for 5 days before the infusion. The [15N]lysine was administered at a constant rate in an amino acid solution with a nitrogen content of 0-96 mol/l, which constituted the sole source of exogenous nitrogen during the infusion. 3. A plateau level of plasma free [15N]lysine enrichment was achieved after infusion for 14 h. The total plasma lysine flux calculated from the plateau was 7-3 mmol/h (range 4-8-9-6). Total body protein turnover calculated from the lysine flux was 3-5 g day-1 kg body wt.-1 (range 2-5-5-0). 4. Muscle sarcoplasmic and myofibrillar fractions were separated, purified and the 15N enrichment was measured. The sarcoplasmic protein fractional synthetic rate was calculated as 3-8%/day (range 2-2-5-1). The myofibrillar protein synthetic rate was 1-46%/day (range 1-09-2-44). 5. Muscle mass, calculated from 24 h creatinine excretion, was 33-7 kg (range 28-8-37-4), which represented 50-0% of body weight (range 38-9-58-1). Total muscle protein synthesis was calculated to account for 53-2% (range 39-5-62-1) of total body protein syntehsis. 6. The advantages and limitations of using continuous infusion of [15N]lysine in human subjects are discussed.
Clin Sci Mol Med 1975 Dec
PMID:Measurement of muscle protein synthetic rate from serial muscle biopsies and total body protein turnover in man by continuous intravenous infusion of L-(alpha-15N)lysine. 120 89

Cationic amino acids, arginine and lysine partition differentially from water into aqueous micellar sodium dodecanoate. Conversely, partitioning of serine, glycine, aspartic acid, glutamic acid, threonine, alanine, proline, valine, leucine, phenylalanine and isoleucine do not vary appreciably. Partitioning from neat hexane into dodecylammonium propionate trapped water in hexane is, however, dependent upon both electrostatic and hydrophobic interactions. These results imply that the interior of dedecylammonium propionate aggregates is negatively charged and is capable of hydrogen bonding in addition to providing a hydrophobic enviroment. The solubilities of amino acids in neat hexane substantiate the previously derived amino acid hydrophobicity scale. Relevance of partitioning in these systems to the postulated selective amino acid compartmentalization is discussed.
J Mol Evol 1975 Nov 04
PMID:Compartmentalization of amino acids in surfactant aggregates. Partitioning between water and aqueous micellar sodium deodecanoate and between hexane and dodecylammonium propionate trapped water in hexane. 120 27

The spatial structure of methylamide N-acetyl-L-argine was studied taking into account the non-valent and electrostati interactions, the torsion energy, and the distorsion of valency angles. Calculation of the favourable conformations of the molecule was carried out with the use of all the combinations of angles phi, psi, chi1 divided by chi4 as an intital approximation. These correspond to the low energy forms of the main chain and to the minima of the torsion potentials of the side chain. Conformational possibilities of arginine and lysine were compared. The calculated stable conformation of N-acetyl-L-arginine-methylamide are compared with the geometry of arginine residues in the proteins with known structure.
Mol Biol (Mosk)
PMID:[Theoretical conformational analysis of methylamide N-acetyl-L-arginine]. 121 9

The spatial structure of the methylamide of N-acetyl-L-lysine has been analysed taking into account non-bonded and electrostatic interactions, torsional energy, bond angles distortion and hydrogen bonding. Conformational capacities of the backbone and mutual dependence of spatial structures of the backbone and the side chain was described by conformational maps obtained by energy minimisation, the dihedral angles and the bond angles of the side chain being varied for every phi, psi point. Every possible combination for phi, psi, x1-x5-angles was used corresponding to the stable form of the backbone and to torsion potential minima of the initial approximations in the calculation of preferred conformations of the molecule. Comparisons are made between stable forms of the methylamide of N-acetyl-L-lysine and Lys residues in proteins with known structure.
Mol Biol (Mosk)
PMID:[Theoretical conformational analysis of methylamide of N-acetyl-L-lysine]. 121 93

Changes of quaternary structure and conformation of molecule concomitant with inactivation were observed in the course of aspartate transaminase acylation by maleic, citraconic, dimethylmaleic and succinic anhydrides. It was established that acylation of 10-12 xi-amino groups of lysine did not induce the dissociation of transaminase into subunits. Further acylation of amino groups (2 groups if dimethylmaleic anhydrade was used as acylating agent) induced dissociation of transaminase dimer into subunits. These data were obtained by sedimentation analysis. The dissociation was accompanied with a sharp decrease of correlation time (from 18 nsec to 9 nsec) of the paramagnetic label covalently bound to the protein. The obtained results allow us to distinguish three types of xi-aminogroups of aspartate transaminase: exposed (about 12 residues), "contact" (2 residues) located in the vicinity to complementary surfaces of subunits and buried (about 6 residues). The stepwise inactivation occurred during the acylation as a result of conformational changes or appearance of sterical hindrances in the cataytic site of the enzyme. The thiol groups were not modified in transaminase molecule under experimental conditions used. Aspartate transaminase treated with citraconic or dimethylmaleic anhydride may be deacylated under mild conditions. After reacylation the quaternary structure was reconstituted and catalytic activity was almost fully restored.
Mol Biol (Mosk)
PMID:[The effect of various acylating agents on the catalytic properties and structure of aspartate aminotransferase]. 121 97

Antisense oligonucleotides efficiently inhibit gene expression in vitro; however, the successful therapeutic application of this technology in vivo will require the development of improved delivery systems. In this report we describe a technique that efficiently delivers antisense oligonucleotides into cells using molecular conjugates. This technique, which was initially developed for the delivery of eukaryotic genes, is based on the construction of DNA-protein complexes that are recognized by the liver-specific asialoglycoprotein receptor. Binding of poly(L-lysine)-asialoorosomucoid (AsOR) protein conjugates with phosphorothioate antisense oligonucleotides to chloramphenicol acetyltransferase (CAT) led to the formation of 50- to 150-nm toroids. Exposure of the antisense molecular complexes (3 microM oligonucleotide) to NIH 3T3 cells genetically modified to express both the AsOR receptor and CAT, inhibited CAT expression by 54%, which was completely blocked by excess AsOR. Equivalent inhibition of CAT activity with purified oligonucleotide alone was observed at a 30 microM concentration. Furthermore, examination of the cells using indirect immunofluorescence for the presence of CAT protein showed 28% of cells exposed to the molecular conjugates lacked any detectable CAT enzyme. Cells exposed to oligonucleotide alone showed a highly variable staining pattern, and only a few of the cells were completely void of CAT protein. Together these data demonstrate that molecular conjugates provide a highly specific and efficient system for the delivery of antisense oligonucleotides.
Somat Cell Mol Genet 1992 Nov
PMID:Targeted delivery of antisense oligonucleotides by molecular conjugates. 128 54

Previous calculations of electrostatic interactions in the rhinovirus capsid have identified a subset of histidine residues, paired with lysine or arginine, that may be involved in pH-induced conformational changes related to viral uncoating. Further calculations with the finite difference method, accounting for the dielectric environment of the ionizable groups, suggest that charge burial in the crystal conformation will prevent protonation of these histidine residues in the pentamer-pentamer interface. Calculations with a modelled pentamer-pentamer interface in which three beta-strands are removed recover mildly acidic pKa values for the histidines. These results are discussed in the context of the structural interactions of these three beta-strands, which form a beta-sheet extension from the rest of the capsid, and with regard to the conformation of the homologous beta-sheet extension in poliovirus, which also possesses homologous histidine-lysine/arginine pairs. A model is developed in which the structural stability of the beta-sheet extension is related to the difference in acid stability of rhinovirus and poliovirus. It is suggested that, for poliovirus prior to cell receptor binding, the beta-sheet extension is stable at pH 3, the pentamer-pentamer interface histidines remain buried, and the virus is acid-stable. Cell receptor binding of poliovirus destabilizes the beta-sheet extension and the acid lability that is proposed to result could be involved in viral uncoating. For rhinovirus it is suggested that the observed conformational change in the absence of cell receptor binding involves a further acidic pH-activated process or conformational fluctuations that rearrange the beta-sheet extension and expose the pentamer-pentamer interface histidine residues to the acidic medium. Sequence analysis and electrostatics calculations reveal an aspartic acid in the beta-sheet extension that may have different pKa values in rhinovirus and poliovirus.
J Mol Biol 1992 Jan 05
PMID:Model for the differential stabilities of rhinovirus and poliovirus to mild acidic pH, based on electrostatics calculations. 130 85

Cloning and sequencing of cDNA segments of human TOP2 gene encoding the 170 kDa form of human DNA topoisomerase II show that Arg486 of the enzyme has been mutated to a lysine in the enzyme from two human leukemia cell lines HL-60/AMSA and KBM-3/AMSA, which were independently selected for resistance to the antitumor drug amsacrine (4'-[9-acridinylamino]-methanesulfon-m-anisidide, mAMSA). Sequence identity comparisons between eukaryotic DNA topoisomerase II and bacterial gyrase (bacterial DNA topoisomerase II) indicate that the position of the common mutation observed in mAMSA-resistant human TOP2 corresponds to that of the point mutation nal-31 in the Escherichia coli gyrase B gene, which confers resistance to nalidixic acid. Because mAMSA and nalidixic acid are known to act on their respective targets by a common mechanism of trapping the covalent enzyme-DNA intermediates, these results provide strong evidence that the 170 kDa form of human DNA topoisomerase II is a major cellular target of mAMSA, and that Arg486 of this enzyme is involved in mAMSA-mediated trapping of the covalent enzyme-DNA complex.
J Mol Biol 1992 Feb 20
PMID:Two independent amsacrine-resistant human myeloid leukemia cell lines share an identical point mutation in the 170 kDa form of human topoisomerase II. 131 90

The molecular conformation of ubiquitinated structures and the validity of the N-end rule were examined by simulating the molecular mechanics to ascertain the global energy-minimized structure. We examined the chemical linkage involved in attaching the ubiquitin carboxyl terminus to the N-terminus of three different x-hexapeptides, where x is the amino group of the acceptor peptide--either valine, arginine or glutamic acid--(x-K linkage) and to the epsilon-amino group of lysine of the acceptor hexapeptide x-glu1-his2-lys3-gly4-lys5-val6 (K-K linkage) through the formation of an isopeptide bond. Changes in conformation and molecular stability of the multi-ubiquitinated structures were determined by energy-minimization procedures using the SYBYL program developed by Tripos Associates. In the x-K linkage, the ubiquitin molecule is stretched in the beta-pleated sheets and beta-turns while the alpha-helices expand, as the molecule continues to unfold linearly. In the K-K linkage, the ubiquitin molecules have turned into a u-shaped, semi-circular alignment, contracting into a compact, folded structure.
J Mol Graph 1992 Mar
PMID:Molecular conformation of ubiquitinated structures and the implications for regulatory function. 132 99


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