Relevant bibliographies by topics / Insulin chain-B

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Insulin chain-B'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Insulin chain-B"

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Csaba, G., and P. Kovács. "Influence of imprinting with A and B chains of insulin on binding and functional changes in tetrahymena." Bioscience Reports 10, no. 5 (October 1, 1990): 431–36. http://dx.doi.org/10.1007/bf01152289.

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Insulin and its A and B chain increased the quantity of intracellular PAS-positive material (glycogen) in tetrahymena, whereas the combined A+B chains decreased it. Imprinting—previous interaction—with insulin, its A and B chains in themselves and with the A+B chain increased the hormone binding capacity of tetrahymena, but the functional effect of imprinting (storage or breakdown of glycogen) showed a different tendency with insulin and A+B chain on the one hand, and A chain and B chain on the other. Since the imprinting potential of a molecule promotes the induction of receptor formation, th
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Davies, J. G., A. V. Muir, and R. E. Offord. "Identification of some cleavage sites of insulin by insulin proteinase." Biochemical Journal 240, no. 2 (December 1, 1986): 609–12. http://dx.doi.org/10.1042/bj2400609.

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In a previous study [Muir, Offord & Davies (1986) Biochem. J. 237, 631-637] the chromatographic and electrophoretic behaviour of a major labelled fragment in the degradation of tritiated insulins by insulin proteinase were used to locate the probable sites of cleavage which had produced this fragment. In order to define these cleavage sites more precisely, authentic markers for the fragments which would be produced by cleavages at, or adjacent to, the most likely sites have now been synthesized. These markers were compared with labelled fragments of the A- and B-chains of insulin produced
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YUAN, Ying, Zhao-Hui WANG, and Jian-Guo TANG. "Intra-A chain disulphide bond forms first during insulin precursor folding." Biochemical Journal 343, no. 1 (September 24, 1999): 139–44. http://dx.doi.org/10.1042/bj3430139.

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In this study, we investigated the folding pathway of insulin precursor and compared it with that of insulin-like growth factor I (IGF-I). The intra-A chain disulphide bond was found to form early in insulin precursor folding, whereas the corresponding disulphide bond in IGF-I formed late. Intra-A chain disulphide-bond deleted [A6, A11-Ser] proteins, including proinsulin, insulin, and A chain, were employed for this investigation. Under the same conditions the recombination yield of insulin from S-sulphonates of native A and B chains was 22%, while the yield of [A6, A11-Ser] insulin from S-sul
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MARON, RUTH, NANCY S. BLOGG, MALU POLANSKI, WAYNE HANCOCK, and HOWARD L. WEINER. "Oral Tolerance to Insulin and the Insulin B-Chain." Annals of the New York Academy of Sciences 778, no. 1 (February 1996): 346–57. http://dx.doi.org/10.1111/j.1749-6632.1996.tb21142.x.

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Miller, G. G., J. F. Hoy, and J. W. Thomas. "Insulin B chain functions as an effective competitor of antigen presentation via peptide homologies present in the thymus." Journal of Experimental Medicine 169, no. 6 (June 1, 1989): 2251–56. http://dx.doi.org/10.1084/jem.169.6.2251.

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The B chain of mammalian insulins contains appropriately spaced amino acids that predict recognition by T cells. However, all T cell clones from an HLA-DR1, Dw6 diabetic donor recognize epitopes associated with the A chain, and the B chain was found to inhibit these responses. Effective intramolecular competition at the level of the APC, not a direct effect on the T cell, is responsible for the inhibition. Insulin B chain contains two clusters of amino acid homology with the TCR beta chain and B chain peptides lacking these clusters do not compete for antigen presentation. A hole in the repert
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Budi, Akin, F. Sue Legge, Herbert Treutlein, and Irene Yarovsky. "Electric Field Effects on Insulin Chain-B Conformation." Journal of Physical Chemistry B 109, no. 47 (December 2005): 22641–48. http://dx.doi.org/10.1021/jp052742q.

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PAYNOVICH, RICHARD C., and FREDERICK H. CARPENTER. "OXIDATION OF THE SULFHYDRYL FORMS OF INSULIN A-CHAIN AND B-CHAIN." International Journal of Peptide and Protein Research 13, no. 2 (January 12, 2009): 113–21. http://dx.doi.org/10.1111/j.1399-3011.1979.tb01858.x.

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Klimontov, Vadim Valer'evich, and Natalya Evgen'evna Myakina. "Insulin glargine: pharmacokinetic and pharmacodynamic basis of clinical effect." Diabetes mellitus 17, no. 4 (October 17, 2014): 99–107. http://dx.doi.org/10.14341/dm2014499-107.

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Glargine became the first long-acting insulin analogue. Glargine was designed to meet basal insulin requirements throughout the day with a single injection. Pharmacokinetics of insulin glargine is characterized by biotransformation into metabolites M1 and M2 that transforms the B chain of glargine so it is similar to the B chain of human insulin. Plasma concentrations of active M1 and M2 metabolites have no pronounced peaks during the day, resulting in lower glucose variability and hypoglycaemia risk when compared with NPH insulin. The metabolic activities of M1 and M2 metabolites are similar
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Nedjar, S., G. Humbert, J. Y. Le Deaut, and G. Linden. "Specificity of chymosin on immobilized bovine B-chain insulin." International Journal of Biochemistry 23, no. 3 (January 1991): 377–81. http://dx.doi.org/10.1016/0020-711x(91)90122-4.

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Chrudinová, Martina, Lenka Žáková, Aleš Marek, Ondřej Socha, Miloš Buděšínský, Martin Hubálek, Jan Pícha, Kateřina Macháčková, Jiří Jiráček, and Irena Selicharová. "A versatile insulin analog with high potency for both insulin and insulin-like growth factor 1 receptors: Structural implications for receptor binding." Journal of Biological Chemistry 293, no. 43 (September 13, 2018): 16818–29. http://dx.doi.org/10.1074/jbc.ra118.004852.

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Insulin and insulin-like growth factor 1 (IGF-1) are closely related hormones involved in the regulation of metabolism and growth. They elicit their functions through activation of tyrosine kinase–type receptors: insulin receptors (IR-A and IR-B) and IGF-1 receptor (IGF-1R). Despite similarity in primary and three-dimensional structures, insulin and IGF-1 bind the noncognate receptor with substantially reduced affinity. We prepared [d-HisB24, GlyB31, TyrB32]-insulin, which binds all three receptors with high affinity (251 or 338% binding affinity to IR-A respectively to IR-B relative to insuli
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Dissertations / Theses on the topic "Insulin chain-B"

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Budi, Bunarta Hendra (Akin), and akin budi@rmit edu au. "On the effects of external stresses on protein conformation." RMIT University. School of Applied Sciences, 2006. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20061116.123431.

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The use of electromagnetic devices such as microwave ovens and mobile phones has certainly brought convenience to our lives. At the same time, the proliferation of said devices has increased public awareness of the potential health hazards. It is generally assumed that there is little or no risk associated with the use of electromagnetic devices, based on the small amount of power associated with those devices. However, case studies on animals indicate that the risk cannot be entirely ruled out. It has long been known that proteins are sensitive to stress, arising from various sources suc
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Cepeda, Sarah Shealy. "Metal-Assisted Hydrolysis of Biological Molecules." Digital Archive @ GSU, 2009. http://digitalarchive.gsu.edu/chemistry_diss/32.

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In Chapter I is a general description of novel metal complexes which hydrolytically cleave peptides, proteins, DNA, and other biological molecules. These reagents are becoming the more important as potential therapeutic agents. A panel of ligands was investigated for coordination to ZrIV and other metals in groups 4, 5, and 6 to effect the greatest degree of hydrolysis. Chapter II describes a ZrIV complex which is capable of hydrolyzing a 30 amino acid peptide, insulin chain B, with amino acid specificity. Oxidized insulin chain B peptide was hydrolyzed after only 4 h of treatment at pH 7.0 an
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Gan, Shao MIng. "Marquage fluorescent des protéines pour étudier les enzymes protéolytiques solubles et immobilisées par la cartographie peptidique électrophorétique." Thèse, 2010. http://hdl.handle.net/1866/4510.

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La cartographie peptidique est une méthode qui permet entre autre d’identifier les modifications post-traductionnelles des protéines. Elle comprend trois étapes : 1) la protéolyse enzymatique, 2) la séparation par électrophorèse capillaire (CE) ou chromatographie en phase liquide à haute performance (HPLC) des fragments peptidiques et 3) l’identification de ces derniers. Cette dernière étape peut se faire par des méthodes photométriques ou par spectrométrie de masse (MS). Au cours de la dernière décennie, les enzymes protéolytiques immobilisées ont acquis une grande popularité parce qu’elles p
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Books on the topic "Insulin chain-B"

1

Mirmira, Raghavendra G. The importance of the COOH-terminal B-chain domain of insulin in insulin-receptor interactions. 1991.

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Book chapters on the topic "Insulin chain-B"

1

Barth, T., J. Velek, J. Jiráček, I. Svoboda, J. Barthová, I. Bláha, V. Černá, et al. "Carboxyterminal octapeptide analogues of the B-chain of human insulin." In Peptides 1992, 745–46. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1470-7_341.

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Claasz, Antonia A., Ross A. Bathgate, Nicola F. Dawson, Roger J. Summers, Laszlo Otvos, Geoffrey W. Tregear, and John D. Wade. "Chemical synthesis and relaxin activity of analogues of ovine Insulin 3 containing specific B-chain residue replacements." In Relaxin 2000, 243–46. Dordrecht: Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-017-2877-5_39.

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3

Tsou, Chen-lu. "The Insulin A and B chains contain sufficient structural information to form the native molecule." In Peptides, 195–98. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-010-9066-7_57.

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4

"Enzymatic-Chemical Exchange of Tyrosine (B16) in the B-Chain of Insulin." In Proceedings of the Fifth USSR-FRG Symposium on Chemistry of Peptides and Proteins, Odessa, USSR, May 16–20, 1985, 99–104. De Gruyter, 1986. http://dx.doi.org/10.1515/9783110858846-013.

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5

Wang, Chih-Chen, and Chen-Lu Tsou. "Correct Pairing of Insulin A and B Chains in Solution and the Formation of the Native from the Scrambled Hormone." In Current Biochemical Research in China, 103–13. Elsevier, 1989. http://dx.doi.org/10.1016/b978-0-12-701905-5.50013-4.

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Conference papers on the topic "Insulin chain-B"

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Klasová, Lenka, Štefan Zorad, Jiří Velek, Jan Ježek, Václav Kašička, Jana Barthová, and Tomislav Barth. "Effect of N-methylation of the peptide bond in the C-terminal part of the B-chain of human insulin on biological activity." In VIIth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2001. http://dx.doi.org/10.1135/css200104063.

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You might also be interested in the extended bibliographies on the topic 'Insulin chain-B' for particular source types:
Journal articles
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