PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28598606-3 2017 Here we show, through the use of noncanonical amino acid mutagenesis, that replacement of the proline residue at position 28 of the insulin B-chain (ProB28) by (4S)-hydroxyproline (Hzp) yields an active form of insulin that dissociates more rapidly, and fibrillates more slowly, than the wild-type protein. Proline 94-101 insulin Homo sapiens 132-139 32139596-5 2020 Specifically, we find that proinsulin Tyr-B16, which is a key residue in normal proinsulin dimerization, helps confer dominant-negative behavior of MIDY mutant proinsulin-C(A7)Y. Substitutions of Tyr-B16 with ether Ala, Asp, or Pro in proinsulin-C(A7)Y each decrease the abnormal interactions between the MIDY mutant and proinsulin-WT, rescuing proinsulin-WT export, limiting ER stress, and increasing insulin production in beta-cells and human islets. Proline 228-231 insulin Homo sapiens 27-37 33405562-5 2019 Our results indicate that the fibroin/proline microneedles can act as carriers of insulin. Proline 38-45 insulin Homo sapiens 82-89 28598606-3 2017 Here we show, through the use of noncanonical amino acid mutagenesis, that replacement of the proline residue at position 28 of the insulin B-chain (ProB28) by (4S)-hydroxyproline (Hzp) yields an active form of insulin that dissociates more rapidly, and fibrillates more slowly, than the wild-type protein. Proline 94-101 insulin Homo sapiens 211-218 23351781-6 2013 RESULTS: Plasma glucose and insulin concentrations showed a greater increase in PRO-CHO compared with PRO (P<0.001). Proline 80-83 insulin Homo sapiens 28-35 26811873-6 2016 A metabolic pathway analysis also indicated that insulin affected the metabolism of alanine, aspartate and glutamate, as well as that of arginine and proline. Proline 150-157 insulin Homo sapiens 49-56 27870861-1 2016 We report here interesting synergistic effects of proline and sorbitol, two well-known chemical chaperones, in the inhibition of fibrillation of two proteins, insulin and lysozyme. Proline 50-57 insulin Homo sapiens 159-166 23416304-4 2013 A tiny covalent perturbation consisting in reversal of Pro(B28)-Lys(B29) residues in a human insulin analog is sufficient to prevent this process. Proline 55-58 insulin Homo sapiens 93-100 21659604-4 2011 We found that the phosphorylation response to insulin is largely mTOR dependent and that mTOR exhibits a unique preference for proline, hydrophobic, and aromatic residues at the +1 position. Proline 127-134 insulin Homo sapiens 46-53 21801810-7 2012 The insulin induced translocation of GLUT4 was attenuated by the Y1 receptor agonist [Phe(7),Pro(34)] pNPY, demonstrating an essential role of the Y1 receptor in GLUT4 translocation. Proline 93-96 insulin Homo sapiens 4-11 15123681-9 2004 When IRS-2 Ser/Thr-Pro motif phosphorylation was examined, chronic insulin + high glucose resulted in a 92% increase in IRS-2 Ser/Thr-Pro motif phosphorylation without a change in IRS-2 mass. Proline 19-22 insulin Homo sapiens 67-74 17130464-0 2006 Insulin-mediated phosphorylation of the proline-rich Akt substrate PRAS40 is impaired in insulin target tissues of high-fat diet-fed rats. Proline 40-47 insulin Homo sapiens 0-7 17130464-0 2006 Insulin-mediated phosphorylation of the proline-rich Akt substrate PRAS40 is impaired in insulin target tissues of high-fat diet-fed rats. Proline 40-47 insulin Homo sapiens 89-96 15486046-12 2005 In summary, 1) SHIP-WT and SHIPDeltaIP expression inhibit insulin and PDGF stimulated Ras, MAPK kinase, and MAPK activities; 2) SHIP associates with tyrosine phosphorylated Shc, and the proline-rich sequences in SHIP associate with Grb2 and titrate out SOS to form Shc*Grb2*SHIP complexes; and 3) dissociation of SOS from the Shc*Grb2 complex inhibits Ras GTP loading, leading to decreased signaling through the MAPK pathway. Proline 186-193 insulin Homo sapiens 58-65 16696315-8 2005 Moreover, plasma insulin concentrations at 60 min was lower than those without A variant (P = 0.0275), and both hypertensive Ala/Pro in HOMA-beta (P = 0.0455) and AUC for insulin (P = 0.0473) were higher, and HOMA-IR was lower (P = 0.0375) as compared with hypertensive Pro/Pro subjects. Proline 129-132 insulin Homo sapiens 171-178 20515662-3 2010 We demonstrate that insulin stimulates phosphorylation of tyrosine and threonine/proline residues on the p85 regulatory subunit of PI3K in Huh-7, and HEK 293 cells. Proline 81-88 insulin Homo sapiens 20-27 18991400-9 2008 Alanine mutations of Lys(484), Leu(552), Asp(591), Ile(602), Lys(616), Asp(620), and Pro(621) compromised affinities for insulin 2-5-fold. Proline 85-88 insulin Homo sapiens 121-128 16631425-6 2006 Whereas insulin raised the proline incorporation and the type II collagen synthesis significantly, physiological doses of estradiol did not show significant effects. Proline 27-34 insulin Homo sapiens 8-15 16631425-7 2006 The stimulating effect of insulin on the [(3)H]-proline incorporation or the type II collagen synthesis was significantly suppressed after preincubation of cells with 10(-11) to 10(-9) M estradiol resembling an unfavorable effect for articular cartilage. Proline 48-55 insulin Homo sapiens 26-33 16002803-9 2005 RESULTS: Plasma insulin responses were higher by 299 +/- 64% and 132 +/- 63% in the CHO+PRO trial than in the CHO trial in the diabetic patients and the matched control subjects, respectively (P < 0.001). Proline 88-91 insulin Homo sapiens 16-23 15123681-9 2004 When IRS-2 Ser/Thr-Pro motif phosphorylation was examined, chronic insulin + high glucose resulted in a 92% increase in IRS-2 Ser/Thr-Pro motif phosphorylation without a change in IRS-2 mass. Proline 134-137 insulin Homo sapiens 67-74 15526500-4 2003 The natural sequence in human insulin at this position is proline at B28 and lysine at B29. Proline 58-65 insulin Homo sapiens 30-37 12716762-6 2003 After adjusting for sex, age, and BMI, adult subjects with the genotype Pro/Pro, Pro/Ala, and Ala/Ala, respectively, showed significant decreasing trends in fasting insulin (11.7, 10.3, and 8.8 micro U/ml; P = 0.002) and HOMA-IR (2.4, 2.1, and 1.7; P = 0.006). Proline 72-75 insulin Homo sapiens 165-172 11524020-1 2001 The structure and folding of a novel human insulin mutant, [Thr(B27) --> Pro, Pro(B28) --> Thr]insulin (PT insulin), in aqueous solution and in mixtures of water and 2,2,2-trifluoroethanol (TFE) have been studied by NMR spectroscopy. Proline 76-79 insulin Homo sapiens 43-50 11836319-9 2002 Nondiabetic Caucasians with an Ala allele (Pro/Ala group) were more insulin sensitive than those in the Pro/Pro group, as evidenced by a lower homeostasis model assessment index (5.18 +/- 1.33 vs. 6.54 +/- 0.54; P < 0.05) and lower levels of insulin at both the fasting (132 +/- 27 vs. 165 +/- 12 pmol/liter; P = 0.03) and 2 h (688 +/- 103 vs. 10190 +/- 99 pmol/liter; P = 0.04) time points during the oral glucose tolerance test. Proline 43-46 insulin Homo sapiens 68-75 11836319-9 2002 Nondiabetic Caucasians with an Ala allele (Pro/Ala group) were more insulin sensitive than those in the Pro/Pro group, as evidenced by a lower homeostasis model assessment index (5.18 +/- 1.33 vs. 6.54 +/- 0.54; P < 0.05) and lower levels of insulin at both the fasting (132 +/- 27 vs. 165 +/- 12 pmol/liter; P = 0.03) and 2 h (688 +/- 103 vs. 10190 +/- 99 pmol/liter; P = 0.04) time points during the oral glucose tolerance test. Proline 43-46 insulin Homo sapiens 245-252 12153745-1 2002 OBJECTIVE: To test the physiological properties of human insulin in which the amino acids Thr (B27) and Pro (B28) are interchanged (PT insulin). Proline 104-107 insulin Homo sapiens 57-64 12403639-1 2002 UNLABELLED: Insulin lispro is a recombinant insulin analogue with transposed amino acids (proline and lysine) at positions 28 and 29 near the C-terminus of the B-chain. Proline 90-97 insulin Homo sapiens 12-19 12403639-1 2002 UNLABELLED: Insulin lispro is a recombinant insulin analogue with transposed amino acids (proline and lysine) at positions 28 and 29 near the C-terminus of the B-chain. Proline 90-97 insulin Homo sapiens 44-51 11524020-1 2001 The structure and folding of a novel human insulin mutant, [Thr(B27) --> Pro, Pro(B28) --> Thr]insulin (PT insulin), in aqueous solution and in mixtures of water and 2,2,2-trifluoroethanol (TFE) have been studied by NMR spectroscopy. Proline 76-79 insulin Homo sapiens 101-108 11524020-1 2001 The structure and folding of a novel human insulin mutant, [Thr(B27) --> Pro, Pro(B28) --> Thr]insulin (PT insulin), in aqueous solution and in mixtures of water and 2,2,2-trifluoroethanol (TFE) have been studied by NMR spectroscopy. Proline 81-84 insulin Homo sapiens 43-50 11524020-1 2001 The structure and folding of a novel human insulin mutant, [Thr(B27) --> Pro, Pro(B28) --> Thr]insulin (PT insulin), in aqueous solution and in mixtures of water and 2,2,2-trifluoroethanol (TFE) have been studied by NMR spectroscopy. Proline 81-84 insulin Homo sapiens 101-108 10479347-0 1999 Preparation of a microcrystalline suspension formulation of Lys(B28)Pro(B29)-human insulin with ultralente properties. Proline 68-71 insulin Homo sapiens 83-90 11334419-11 2001 The insulin sensitivity index decreased comparably in Pro/Pro and X/Ala (to 71 +/- 8 vs. 74 +/- 9% of basal, P = 0.8). Proline 54-57 insulin Homo sapiens 4-11 11334419-11 2001 The insulin sensitivity index decreased comparably in Pro/Pro and X/Ala (to 71 +/- 8 vs. 74 +/- 9% of basal, P = 0.8). Proline 58-61 insulin Homo sapiens 4-11 11289057-1 2001 Recent studies have identified a common proline-to-alanine substitution (Pro12Ala) in the peroxisome proliferator-activated receptor-gamma2 (PPAR-gamma2), a nuclear receptor that regulates adipocyte differentiation and possibly insulin sensitivity. Proline 40-47 insulin Homo sapiens 228-235 11843266-0 2001 Relationship between plasma cyclo (His-Pro), a neuropeptide common to processed protein-rich food, and C-peptide/insulin molar ratio in obese women. Proline 39-42 insulin Homo sapiens 103-112 11843266-0 2001 Relationship between plasma cyclo (His-Pro), a neuropeptide common to processed protein-rich food, and C-peptide/insulin molar ratio in obese women. Proline 39-42 insulin Homo sapiens 113-120 11144701-7 2000 DATA SYNTHESIS: Insulin aspart, the second Food and Drug Administration-approved rapid-acting insulin analog, is produced by recombinant technology that replaces the proline at position 28 on the B chain of insulin with negatively charged aspartic acid. Proline 166-173 insulin Homo sapiens 16-23 11144701-7 2000 DATA SYNTHESIS: Insulin aspart, the second Food and Drug Administration-approved rapid-acting insulin analog, is produced by recombinant technology that replaces the proline at position 28 on the B chain of insulin with negatively charged aspartic acid. Proline 166-173 insulin Homo sapiens 207-214 10479347-1 1999 The monomeric analogue, Lys(B28)Pro(B29)-human insulin (LysPro), has been crystallized using similar conditions employed to prepare extended-acting insulin ultralente formulations. Proline 32-35 insulin Homo sapiens 47-54 10490782-10 1999 In addition, individuals found to simultaneously exhibit homozygosity of the common allele of all three polymorphisms (genotypes: Arg/Arg, pro/pro and II/II) exhibited significantly elevated fasting insulin levels (Pc = 0.03). Proline 139-142 insulin Homo sapiens 199-206 10490782-10 1999 In addition, individuals found to simultaneously exhibit homozygosity of the common allele of all three polymorphisms (genotypes: Arg/Arg, pro/pro and II/II) exhibited significantly elevated fasting insulin levels (Pc = 0.03). Proline 143-146 insulin Homo sapiens 199-206 9708987-5 1998 At the monomer-monomer interfaces, the B28 Pro --> Asp mutation leads to increased conformational flexibility in the B chain C termini, resulting in the loss of important intermolecular van der Waals contacts, thus explaining the monomeric character of B28 Asp insulin. Proline 43-46 insulin Homo sapiens 264-271 10332684-1 1999 OBJECTIVE: To quantitate the contribution of postprandial blood glucose, which improves with the short-acting insulin analog lispro [Lys(B28),Pro(B29)] in type 1 diabetes, to the overall 24-h blood glucose concentration and the long-term HbA1c concentration under conditions of different postabsorptive blood glucose. Proline 142-145 insulin Homo sapiens 110-117 10199158-1 1999 Two rapid-acting insulin analogues, Lys(B28), Pro(B29)-human insulin (insulin lispro) and Asp(B28)-human insulin (insulin aspart) are developed and introduced into the clinical trials or applications recently. Proline 46-49 insulin Homo sapiens 17-24 10199158-1 1999 Two rapid-acting insulin analogues, Lys(B28), Pro(B29)-human insulin (insulin lispro) and Asp(B28)-human insulin (insulin aspart) are developed and introduced into the clinical trials or applications recently. Proline 46-49 insulin Homo sapiens 61-68 10199158-1 1999 Two rapid-acting insulin analogues, Lys(B28), Pro(B29)-human insulin (insulin lispro) and Asp(B28)-human insulin (insulin aspart) are developed and introduced into the clinical trials or applications recently. Proline 46-49 insulin Homo sapiens 61-68 10199158-1 1999 Two rapid-acting insulin analogues, Lys(B28), Pro(B29)-human insulin (insulin lispro) and Asp(B28)-human insulin (insulin aspart) are developed and introduced into the clinical trials or applications recently. Proline 46-49 insulin Homo sapiens 61-68 10199158-3 1999 Proline at position B28 near the COOH terminal of the B chain of human insulin is important for the dimerization of insulin molecules. Proline 0-7 insulin Homo sapiens 71-78 10199158-3 1999 Proline at position B28 near the COOH terminal of the B chain of human insulin is important for the dimerization of insulin molecules. Proline 0-7 insulin Homo sapiens 116-123 10051177-9 1999 Insulin lispro, a recombinant insulin analogue, is identical to human insulin except for the transposition of proline and lysine at positions 28 and 29 in the C-terminus of the B chain. Proline 110-117 insulin Homo sapiens 0-7 15991899-1 1997 Insulin lispro (Humalog) is a biosynthetic insulin analogue in which the positions of proline and lysine are reversed in the C-terminal portion of the B chain. Proline 86-93 insulin Homo sapiens 0-7 9620104-2 1998 Inversion of the proline-lysine amino acid sequence at positions 28 and 29 on the B chain is responsible for its more rapid absorption, faster onset, and shorter duration of action compared with regular insulin. Proline 17-24 insulin Homo sapiens 203-210 9428692-3 1997 We show that interaction between Stat 5B and the receptor requires a functional insulin-receptor kinase, Tyr960 of insulin receptor is implicated in the interaction with Stat 5B, whereas asparagine and proline forming the NPEY960-motif are not, and Stat 5B mutated at Thr684, a potential phosphorylation site of mitogen-activated protein kinase, loses its ability to interact with the insulin receptor. Proline 202-209 insulin Homo sapiens 80-87 9410552-4 1997 The Lilly Laboratories, by inverting the amino acids lysine and proline in positions 28 and 29 in the B chain, have created an insulin (Lispro) which more rapidly dissociates into monomers after injection. Proline 64-71 insulin Homo sapiens 127-134 9710993-2 1998 The natural sequence in human insulin at these positions is proline at B28 and lysine at B29. Proline 60-67 insulin Homo sapiens 30-37 9677011-1 1998 Insulin lispro is a newly developed analogue of human insulin where the positions of the amino acids lysine and proline have been switched at the end of the B chain of the insulin molecule. Proline 112-119 insulin Homo sapiens 0-7 9677011-1 1998 Insulin lispro is a newly developed analogue of human insulin where the positions of the amino acids lysine and proline have been switched at the end of the B chain of the insulin molecule. Proline 112-119 insulin Homo sapiens 54-61 9677011-1 1998 Insulin lispro is a newly developed analogue of human insulin where the positions of the amino acids lysine and proline have been switched at the end of the B chain of the insulin molecule. Proline 112-119 insulin Homo sapiens 172-179 9677011-2 1998 Insulin lispro with lysine at position B28 and proline at position B29 has a weaker tendency for self-association than human insulin. Proline 47-54 insulin Homo sapiens 125-132 9374504-1 1997 We have recently reported (1) that two naturally occurring mutants of the insulin receptor tyrosine kinase domain, Arg-1174 --> Gln and Pro-1178 --> Leu (Gln-1174 and Leu1178, respectively), both found in patients with inherited severe insulin resistance, markedly impaired receptor tyrosine autophosphorylation, with both mutant receptors being unable to mediate the stimulation of glycogen synthesis or mitogenesis by insulin when expressed in Chinese hamster ovary cells. Proline 139-142 insulin Homo sapiens 74-81 9374504-1 1997 We have recently reported (1) that two naturally occurring mutants of the insulin receptor tyrosine kinase domain, Arg-1174 --> Gln and Pro-1178 --> Leu (Gln-1174 and Leu1178, respectively), both found in patients with inherited severe insulin resistance, markedly impaired receptor tyrosine autophosphorylation, with both mutant receptors being unable to mediate the stimulation of glycogen synthesis or mitogenesis by insulin when expressed in Chinese hamster ovary cells. Proline 139-142 insulin Homo sapiens 242-249 9374504-1 1997 We have recently reported (1) that two naturally occurring mutants of the insulin receptor tyrosine kinase domain, Arg-1174 --> Gln and Pro-1178 --> Leu (Gln-1174 and Leu1178, respectively), both found in patients with inherited severe insulin resistance, markedly impaired receptor tyrosine autophosphorylation, with both mutant receptors being unable to mediate the stimulation of glycogen synthesis or mitogenesis by insulin when expressed in Chinese hamster ovary cells. Proline 139-142 insulin Homo sapiens 242-249 9434806-0 1997 Safety and efficacy of [Lys(B28), Pro(B29)]-human insulin in patients with diabetes mellitus. Proline 34-37 insulin Homo sapiens 50-57 9339963-1 1997 Insulin lispro, a recombinant insulin analogue, is identical to human insulin except for the transposition of proline and lysine at positions 28 and 29 in the C-terminus of the B chain. Proline 110-117 insulin Homo sapiens 0-7 15991899-1 1997 Insulin lispro (Humalog) is a biosynthetic insulin analogue in which the positions of proline and lysine are reversed in the C-terminal portion of the B chain. Proline 86-93 insulin Homo sapiens 43-50 9088775-1 1997 Lys(B28)Pro(B29) human insulin analogue (Lispro) is a newly developed monomeric insulin analogue with a rapid onset and short duration of action. Proline 8-11 insulin Homo sapiens 23-30 9248708-2 1997 For some short acting insulin analogues, in particular for [Lys(B28),Pro(B29)]-human insulin, preclinical and clinical trials have been performed. Proline 69-72 insulin Homo sapiens 22-29 9248708-2 1997 For some short acting insulin analogues, in particular for [Lys(B28),Pro(B29)]-human insulin, preclinical and clinical trials have been performed. Proline 69-72 insulin Homo sapiens 85-92 9141561-3 1997 DNA was extracted, the insulin gene amplified by the PCR, and by direct sequencing, a novel point mutation, G1552C, was identified, which resulted in the substitution of proline (CCT) for arginine (CGT) at position 65. Proline 170-177 insulin Homo sapiens 23-30 9088775-1 1997 Lys(B28)Pro(B29) human insulin analogue (Lispro) is a newly developed monomeric insulin analogue with a rapid onset and short duration of action. Proline 8-11 insulin Homo sapiens 80-87 8840095-1 1996 The time-action profile of the insulin analogue insulin lispro ([Lys(B28), Pro(B29)] human insulin) with its rapid onset and short duration of action might be more suitable to limit hyperglycaemic excursions after a meal rich in rapidly absorbable carbohydrates in comparison to regular human insulin. Proline 75-78 insulin Homo sapiens 31-38 8922361-1 1996 Insulin lispro [Lys (B28), Pro (B29) human insulin] is a rapidly absorbed analog that has diminished tendency to self-associate. Proline 27-30 insulin Homo sapiens 0-7 8922361-1 1996 Insulin lispro [Lys (B28), Pro (B29) human insulin] is a rapidly absorbed analog that has diminished tendency to self-associate. Proline 27-30 insulin Homo sapiens 43-50 8840095-1 1996 The time-action profile of the insulin analogue insulin lispro ([Lys(B28), Pro(B29)] human insulin) with its rapid onset and short duration of action might be more suitable to limit hyperglycaemic excursions after a meal rich in rapidly absorbable carbohydrates in comparison to regular human insulin. Proline 75-78 insulin Homo sapiens 48-55 8840095-1 1996 The time-action profile of the insulin analogue insulin lispro ([Lys(B28), Pro(B29)] human insulin) with its rapid onset and short duration of action might be more suitable to limit hyperglycaemic excursions after a meal rich in rapidly absorbable carbohydrates in comparison to regular human insulin. Proline 75-78 insulin Homo sapiens 48-55 8840095-1 1996 The time-action profile of the insulin analogue insulin lispro ([Lys(B28), Pro(B29)] human insulin) with its rapid onset and short duration of action might be more suitable to limit hyperglycaemic excursions after a meal rich in rapidly absorbable carbohydrates in comparison to regular human insulin. Proline 75-78 insulin Homo sapiens 48-55 8821525-1 1996 [Lys(B28),Pro(B29)]-human insulin (insulin lispro, CAS 133107-64-9, LY275585, Humalog) is a quick acting insulin analog which is currently undergoing clinical evaluation for the treatment of diabetes. Proline 10-13 insulin Homo sapiens 26-33 8648633-9 1996 The structure reveals that the lost ability of des-[Phe(B25)] insulin to self-associate is caused by a conformational change of the C-terminal region of the B-chain, which results in an intra-molecular hydrophobic interaction between Pro(B28) and the hydrophobic region Leu(B11)-Leu(B15) of the B-chain alpha-helix. Proline 234-237 insulin Homo sapiens 62-69 7705764-2 1994 To overcome these problems, the short-acting human insulin analogue [LYS(B28),PRO(B29)] (LYSPRO) was developed. Proline 78-81 insulin Homo sapiens 51-58 7586939-0 1995 [Lys(B28), Pro(B29)]-human insulin: effect of injection time on postprandial glycemia. Proline 11-14 insulin Homo sapiens 27-34 7586939-1 1995 BACKGROUND: [Lys(B28), Pro(B29)]-human insulin (lispro) is an insulin analogue with a reduced capacity for self-association and faster absorption from subcutaneous injection sites. Proline 23-26 insulin Homo sapiens 39-46 7586939-1 1995 BACKGROUND: [Lys(B28), Pro(B29)]-human insulin (lispro) is an insulin analogue with a reduced capacity for self-association and faster absorption from subcutaneous injection sites. Proline 23-26 insulin Homo sapiens 62-69 7665623-6 1995 The autophosphorylation of Pro-87 IR was less sensitive to insulin than that of Leu-87 IR, suggesting the reduced insulin binding affinity. Proline 27-30 insulin Homo sapiens 59-66 7665623-6 1995 The autophosphorylation of Pro-87 IR was less sensitive to insulin than that of Leu-87 IR, suggesting the reduced insulin binding affinity. Proline 27-30 insulin Homo sapiens 114-121 7958544-0 1994 Pharmacokinetics, pharmacodynamics and glucose counterregulation following subcutaneous injection of the monomeric insulin analogue [Lys(B28),Pro(B29)] in IDDM. Proline 142-145 insulin Homo sapiens 115-122 7713281-0 1994 Lack of in vitro complement activation by the human insulin analogue LYS(b28)PRO(B29) Proline 77-80 insulin Homo sapiens 52-59 2693157-6 1989 Thus, the two derivatives specifically modified the cellular processing of insulin in cultured fetal hepatocytes, and exerted an insulin-like effect on glycogenesis clearly enhanced through modification of DP-432 by substitution of glycine for proline (DP-640). Proline 244-251 insulin Homo sapiens 129-136 2164929-1 1990 We have recently described an insulin-resistant patient with leprechaunism (leprechaun G.) having a homozygous leucine----proline mutation at amino acid position 233 in the alpha-chain of the insulin receptor. Proline 122-129 insulin Homo sapiens 30-37 34560246-2 2021 This emerging evidence points to the importance of pro-oxidation as an important stimulus for endurance-training adaptations, including mitochondrial biogenesis, endogenous antioxidant production, insulin signalling, angiogenesis and growth factor signaling. Proline 51-54 insulin Homo sapiens 197-204 8314011-0 1994 [Lys(B28), Pro(B29)]-human insulin. Proline 11-14 insulin Homo sapiens 27-34 8314011-2 1994 [Lys(B28, Pro(B29)]-human insulin (LYSPRO) is an insulin analogue in which the natural amino acid sequence of the B-chain at positions 28 and 29 is inverted. Proline 10-13 insulin Homo sapiens 26-33 8314011-2 1994 [Lys(B28, Pro(B29)]-human insulin (LYSPRO) is an insulin analogue in which the natural amino acid sequence of the B-chain at positions 28 and 29 is inverted. Proline 10-13 insulin Homo sapiens 49-56 1419149-0 1992 Effect of insulin on the proline transport activity in cultured fibroblasts from patients with Werner syndrome. Proline 25-32 insulin Homo sapiens 10-17 1419149-1 1992 The effect of insulin on the transport of proline has been studied in cultured fibroblasts from normal individuals, non-insulin-dependent diabetic patients, and patients with Werner syndrome. Proline 42-49 insulin Homo sapiens 14-21 2479553-0 1989 A leucine-to-proline mutation in the insulin receptor in a family with insulin resistance. Proline 13-20 insulin Homo sapiens 37-44 2479553-10 1989 These observations show a linkage between the leucine-to-proline mutation and the observed insulin resistance in this family. Proline 57-64 insulin Homo sapiens 91-98 3510558-8 1986 For isoleucine and proline, the insulin levels required for a half-maximal response were less than for glucose disposal (P less than 0.05), but, for all other insulin-influenced AA, the levels required were similar to those for glucose disposal. Proline 19-26 insulin Homo sapiens 32-39 2566520-9 1989 Insulin decreased always BCAA but also threonine, proline, tyrosine, methionine and total aminoacid levels. Proline 50-57 insulin Homo sapiens 0-7 6997175-2 1980 As expected, the infusion of insulin exhibited significant reduction of the release of glycine, proline, valine, phenylalanine, leucine, threonine and isoleucine. Proline 96-103 insulin Homo sapiens 29-36 33369793-14 2021 Immunoblotting assays showed that the phosphorylation levels of AMP-activated protein kinase, a rate-limiting factor in insulin-independent signaling, and that of liver kinase B1, an upstream factor of AMP-activated protein kinase, in both milk casein hydrolysate and isoleucine-proline-proline-treated cells were higher than those in the control cells. Proline 279-286 insulin Homo sapiens 120-127 33369793-14 2021 Immunoblotting assays showed that the phosphorylation levels of AMP-activated protein kinase, a rate-limiting factor in insulin-independent signaling, and that of liver kinase B1, an upstream factor of AMP-activated protein kinase, in both milk casein hydrolysate and isoleucine-proline-proline-treated cells were higher than those in the control cells. Proline 287-294 insulin Homo sapiens 120-127 33369793-17 2021 The findings of our study suggest that milk casein hydrolysate enhances glucose uptake by activating insulin-independent AMP-activated protein kinase signaling in skeletal muscle cells, which might be mediated by a milk casein hydrolysate-derived peptide, namely, isoleucine-proline-proline. Proline 275-282 insulin Homo sapiens 101-108 33369793-17 2021 The findings of our study suggest that milk casein hydrolysate enhances glucose uptake by activating insulin-independent AMP-activated protein kinase signaling in skeletal muscle cells, which might be mediated by a milk casein hydrolysate-derived peptide, namely, isoleucine-proline-proline. Proline 283-290 insulin Homo sapiens 101-108