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  • 1
    Electronic Resource
    Electronic Resource
    Improvement in the oxidative folding of endothelin-1 by a lys-Arg extension at the amino terminus: Implication of a salt bridge between Arg−1 and Asp8 (1997)
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 185-192 
    Details
    ISSN: 1573-3904
    Keywords: α-Helix ; Carboxamide substitution ; Circular dichroism ; Disulfide isomer ; KR-ET-1 ; Prosequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary An amino-terminal extension of endothelin-l by the lys-Arg dipeptide in the prosequence (KR-ET-1) greatly increased the ratio of native-type to non-native-type disulfide isomer (96/4 versus 71/29) during the oxidative folding reaction. This improvement was completely abolished by substituting Asn for Asp at position 8 (D8N-KR-ET-1), whereas most of it was maintained with similar carboxamide analogues replaced at Glu10 or Asp18. Structure analyses by circular dichroism spectroscopy revealed that (i) in the carboxylate state, the α-helical content of the native-type isomer of KR-ET-l is higher than that of the native-type isomer of ET-1, while such a variation is not observed in the corresponding non-native-type isomer of KR-ET-l; and (ii) the enhanced α-helicity resulting from the Lys-Arg extension is largely diminished in D8N-KR-ET-l. From these results and our previous findings that the helical structure in KR-ET-l is stabilized by a particular salt bridge between the extended Arg−1 basic moiety and either the Asp8 or Glu10 acidic side chain in Et-1 [Aumelas, A. et al., Biochemistry, 34 (1995) 4546], we conclude that the formation of a specific salt bridge between the side chains of Arg−1 and Asp8 in KR-ET-1 is critical for the predominant generation of the native-type disulfide isomer, probably because it stabilizes the helical structure of parental ET-1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443532
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  • 2
    Electronic Resource
    Electronic Resource
    Improvement in the oxidative folding of endothelin-1 by a Lys-Arg extension at the amino terminus: Implication of a salt bridge between Arg-1 and Asp8 (1997)
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 185-192 
    Details
    ISSN: 1573-3904
    Keywords: α-Helix ; Carboxamide substitution ; Circular dichroism ; Disulfide isomer ; KR-ET-1 ; Prosequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract An amino-terminal extension of endothelin-1 by the Lys-Arg dipeptide in the prosequence (KR-ET-1) greatly increased the ratio of native-type to non-native-type disulfide isomer (96/4 versus 71/29) during the oxidative folding reaction. This improvement was completely abolished by substituting Asn for Asp at position 8 (D8N-KR-ET-1), whereas most of it was maintained with similar carboxamide analogues replaced at Glu10 or Asp18. Structure analyses by circular dichroism spectroscopy revealed that (i) in the carboxylate state, the α-helical content of the native-type isomer of KR-ET-1 is higher than that of the native-type isomer of ET-1, while such a variation is not observed in the corresponding non-native-type isomer of KR-ET-1; and (ii) the enhanced α-helicity resulting from the Lys-Arg extension is largely diminished in D8N-KR-ET-1. From these results and our previous findings that the helical structure in KR-ET-1 is stabilized by a particular salt bridge between the extended Arg-1 basic moiety and either the Asp8 or Glu10 acidic side chain in ET-1 [Aumelas, A. et al., Biochemistry, 34 (1995) 4546], we conclude that the formation of a specific salt bridge between the side chains of Arg-1 and Asp8 in KR-ET-1 is critical for the predominant generation of the native-type disulfide isomer, probably because it stabilizes the helical structure of parental ET-1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008835323518
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  • 3
    Electronic Resource
    Electronic Resource
    Synthesis and disulfide structure determination of conotoxin GS, a γ-carboxyglutamic acid-containing neurotoxic peptide (1995)
    Springer
    International journal of peptide research and therapeutics 2 (1995), S. 17-26 
    Details
    ISSN: 1573-3904
    Keywords: Conotoxin GS ; γ-Carboxyglutamic acid ; Solution synthesis ; Disulfide structure ; Disulfide isomer ; CD spectrum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Conotoxin GS, a γ-carboxyglutamic acid(Gla)-containing neurotoxic peptide composed of 34 amino acid residues with one Gla residue and three intramolecular disulfide bonds, was synthesized in solution by the Boc strategy, using the cyclohexyl group to protect the γ,γ-dicarboxyl functional side chain of the Gla residue. All of the protecting groups were removed by the HF procedure. During the synthesis, the Gla residue was completely stable and decarboxylated product was observed. The free peptide was subjected to the oxidative folding reaction. The reaction proceeded almost quantitatively in the presence of reduced and oxidized glutathione; however, no product was formed in the absence of redox reagents concomitant with the formation of disulfide isomers or intermediates. The final product was confirmed to be identical to natural conotoxin GS on reversed phase- and ion exchange-HPLC as well as capillary zone electrophoresis. The disulfide structure of synthetic conotoxin GS was determined by gas-phase sequencing and mass spectrometry of its proteolytic fragments and was found to be identical to those of other ω-conotoxins. The major disulfide isomer obtained during the oxidative folding reaction without redox reagents was determined in the same manner. To clarify the role of the Gla residue and the disulfide structure in the conotoxin GS molecule, decarboxylated conotoxin GS and its disulfide isomer were also synthesized, and the neurotoxic activities and circular dichroism spectra of these peptides were compared with those of conotoxin GS and its disulfide isomer. The results showed that the correct disulfide structure was necessary for expression of the toxicity; however, the presence of the Gla residue was not a prerequisite for both the activity and the calcium-dependent conformational transition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00122919
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation and characteristics of yeasts able to grow at low concentrations of nutrients (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 14 (1998), S. 233-238 
    Details
    ISSN: 0749-503X
    Keywords: Oligotrophic yeasts ; low-nutrient conditions ; starvation ; Cryptococcaceae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Seven oligotrophic yeasts, which can grow in a 104-fold dilution of malt-yeast-glucose-peptone medium (10-4 YM), were mainly isolated from soil. These yeasts belong to the Cryptococcaceae. When inoculated at about 102 cells/ml in 10-4 YM, the isolates grew to 1·4×103-2·4×105 cells/ml after 3 days. Some culture collection yeasts fell into three groups according to their growth characteristics in 10-4 YM, one group showing characteristics of the oligotrophic yeasts. The half-saturation values of uptake by the five isolated oligotrophic yeasts for D-glucose, L-leucine and L-amino acids were 6·0-25·0, 1·7-43·3 and 3·5-21·6 μM, respectively. The oligotrophic yeasts suspended in 10 mM-phosphate buffer (pH 6·0) had high tolerances for starvation, and remained more than 15% viable after 90 days of starvation. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 5
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    daf-2, an insulin receptor-like gene that regulates longevity and diapause in Caenorhabditis elegans (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-15
    Description: A C. elegans neurosecretory signaling system regulates whether animals enter the reproductive life cycle or arrest development at the long-lived dauer diapause stage. daf-2, a key gene in the genetic pathway that mediates this endocrine signaling, encodes an insulin receptor family member. Decreases in DAF-2 signaling induce metabolic and developmental changes, as in mammalian metabolic control by the insulin receptor. Decreased DAF-2 signaling also causes an increase in life-span. Life-span regulation by insulin-like metabolic control is analogous to mammalian longevity enhancement induced by caloric restriction, suggesting a general link between metabolism, diapause, and longevity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kimura, K D -- Tissenbaum, H A -- Liu, Y -- Ruvkun, G -- R01AG14161/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1997 Aug 15;277(5328):942-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9252323" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Amino Acid Sequence ; Animals ; Caenorhabditis elegans/chemistry/*genetics/growth & development/metabolism ; Caenorhabditis elegans Proteins ; Chromosome Mapping ; Conserved Sequence ; Energy Intake ; *Genes, Helminth ; Glucose/metabolism ; Humans ; Insulin/metabolism ; Larva/genetics/growth & development/metabolism ; Longevity/*genetics ; Molecular Sequence Data ; Mutation ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositol Phosphates/metabolism ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Receptor, IGF Type 1/chemistry/genetics ; Receptor, Insulin/chemistry/*genetics/metabolism ; Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 6
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    Phosphorylation and activation of 13S condensin by Cdc2 in vitro (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-17
    Description: 13S condensin is a multisubunit protein complex essential for mitotic chromosome condensation in Xenopus egg extracts. Purified 13S condensin introduces positive supercoils into DNA in the presence of topoisomerase I and adenosine triphosphate in vitro. The supercoiling activity of 13Scondensin was regulated by mitosis-specific phosphorylation. Immunodepletion, in vitro phosphorylation, and peptide-mapping experiments indicated that Cdc2 is likely to be the kinase that phosphorylates and activates 13S condensin. Multiple Cdc2 phosphorylation sites are clustered in the carboxyl-terminal domain of the XCAP-D2 (Xenopus chromosome-associated polypeptide D2) subunit. These results suggest that phosphorylation of 13Scondensin by Cdc2 may trigger mitotic chromosome condensation in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kimura, K -- Hirano, M -- Kobayashi, R -- Hirano, T -- CA45508/CA/NCI NIH HHS/ -- GM53926/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 16;282(5388):487-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, Post Office Box 100, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9774278" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/chemistry/*metabolism ; Amino Acid Sequence ; Animals ; CDC2 Protein Kinase/*metabolism ; Chromosomes/chemistry/*metabolism ; DNA, Circular/chemistry/metabolism ; DNA, Superhelical/*chemistry ; DNA-Binding Proteins/chemistry/*metabolism ; Enzyme Activation ; Interphase ; *Mitosis ; Molecular Sequence Data ; Multiprotein Complexes ; Nucleic Acid Conformation ; Peptide Mapping ; Phosphorylation ; Xenopus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 7
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    Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase) (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-12
    Description: The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP.RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kimura, K -- Ito, M -- Amano, M -- Chihara, K -- Fukata, Y -- Nakafuku, M -- Yamamori, B -- Feng, J -- Nakano, T -- Okawa, K -- Iwamatsu, A -- Kaibuchi, K -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):245-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Signal Transduction, Nara Institute of Science and Technology, Ikoma 630-01, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662509" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Actins/metabolism ; Amino Acid Sequence ; Animals ; Cattle ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/*metabolism ; Intracellular Signaling Peptides and Proteins ; Isopropyl Thiogalactoside/pharmacology ; Mice ; Molecular Sequence Data ; Muscle Contraction ; Muscle, Smooth/physiology ; Myosin Light Chains/metabolism ; Myosin-Light-Chain Phosphatase ; Oxazoles/pharmacology ; Phosphoprotein Phosphatases/*antagonists & inhibitors/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/*metabolism ; rho-Associated Kinases ; rhoA GTP-Binding Protein
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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