PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 6188161-6 1983 Preincubation with several concentrations of insulin increased the 32P incorporation into this peptide in dose-dependent fashion, whereas insulin-like growth factors were approximately equal to 2% as potent and epidermal growth factor had little or no effect, consistent with their known affinities for the insulin receptor. Phosphorus-32 67-70 insulin Homo sapiens 45-52 6292721-2 1983 Peripheral leukocyte DNA from 217 unrelated persons, including blacks, whites, and Pima Indians, was analyzed by restriction-enzyme digestion, blotting to nitrocellulose filters, and hybridization to cloned [32P]insulin-gene probes. Phosphorus-32 208-211 insulin Homo sapiens 212-219 6340724-2 1983 Half-maximal stimulation of 32P incorporation occurs at (2-3) X 10(-9) M insulin, a concentration identical with the Kd for insulin binding in this preparation. Phosphorus-32 28-31 insulin Homo sapiens 73-80 6340724-2 1983 Half-maximal stimulation of 32P incorporation occurs at (2-3) X 10(-9) M insulin, a concentration identical with the Kd for insulin binding in this preparation. Phosphorus-32 28-31 insulin Homo sapiens 124-131 6286669-1 1982 32P-labeled ATP-citrate lyase isolated from 32P-labeled hepatocytes treated with insulin contained 1.6-1.8-fold greater 32P-radioactivity per mg protein than control enzyme. Phosphorus-32 0-3 insulin Homo sapiens 81-88 6757253-2 1982 Addition of insulin to Triton-solubilized extracts of human placental membranes selectively stimulates the incorporation of 32P from [gamma-32P]ATP into an endogenous 95,000-dalton protein, which is identified as a component of the insulin receptor by immunoprecipitation. Phosphorus-32 124-127 insulin Homo sapiens 12-19 6757253-3 1982 The insulin-stimulated increment in 32P is recovered largely in [32P]tyrosine after acid hydrolysis. Phosphorus-32 36-39 insulin Homo sapiens 4-11 6757253-3 1982 The insulin-stimulated increment in 32P is recovered largely in [32P]tyrosine after acid hydrolysis. Phosphorus-32 65-68 insulin Homo sapiens 4-11 6286669-1 1982 32P-labeled ATP-citrate lyase isolated from 32P-labeled hepatocytes treated with insulin contained 1.6-1.8-fold greater 32P-radioactivity per mg protein than control enzyme. Phosphorus-32 44-47 insulin Homo sapiens 81-88 6286669-1 1982 32P-labeled ATP-citrate lyase isolated from 32P-labeled hepatocytes treated with insulin contained 1.6-1.8-fold greater 32P-radioactivity per mg protein than control enzyme. Phosphorus-32 44-47 insulin Homo sapiens 81-88 6286669-5 1982 The site of insulin-directed phosphorylation of ATP-citrate lyase (Thr-Ala-Ser(32P)-Phe-Ser-Glu-Ser-Arg) is the same as that directed by glucagon, and, in turn, identical with that phosphorylated by the cAMP-dependent protein kinase in vitro. Phosphorus-32 79-82 insulin Homo sapiens 12-19 6286669-3 1982 Quantitative high performance liquid chromatographic peptide mapping of the tryptic digests revealed a principal 32P-peptide which accounted for at least 80% of the insulin induced increment in 32P-radioactivity of native lyase. Phosphorus-32 113-116 insulin Homo sapiens 165-172 6123319-11 1982 Results obtained show that the exposure of fat-cells to insulin leads to a 5-fold increase in incorporation of 32P into a peptide which is different from those most markedly affected after exposure of fat-cells to adrenaline. Phosphorus-32 111-114 insulin Homo sapiens 56-63 7035458-4 1982 Insulin (1 milliunit/ml) increases the 32P content of immunoprecipitated lyase 2- to 3-fold in 10 min. Phosphorus-32 39-42 insulin Homo sapiens 0-7 7035458-5 1982 Over 90% of acid-stable 32P on lyase is 32P-serine in enzyme isolated from both control and insulin-treated cells. Phosphorus-32 24-27 insulin Homo sapiens 92-99 176155-7 1976 When present as the sole hormone, insulin (100 microunits/ml) consistently and selectively stimulated the 32P incorporation into a peptide of molecular weight 123,000 (endoplasmic reticulum, cytoplasm) without significant alteration in the 32P content of any other major peptide. Phosphorus-32 106-109 insulin Homo sapiens 34-41 7012140-1 1981 Physiological concentrations of insulin stimulate the incorporation of 32P into ribosomal protein S6 in intact 3T3-L1 adipocytes (Smith, C. J., Wejksnora, P. J., Warner, J. Phosphorus-32 71-74 insulin Homo sapiens 32-39 7012140-8 1981 Extracts from cells treated with insulin also exhibit an increased ability to incorporate 32P from [gamma-32P]ATP into protein S6 in vitro (Smith, C. J., Rubin, C. S., and Rosen, O. M. (1980) Proc. Phosphorus-32 90-93 insulin Homo sapiens 33-40 7012140-14 1981 We now report that the direct addition of insulin to particulate preparations containing high affinity insulin receptors and ribosomes derived from insulin-sensitive cells (not previously exposed to insulin) stimulates incorporation of 32P from [gamma-32P]ATP into ribosomal protein S6 1.5- to 3.0-fold. Phosphorus-32 236-239 insulin Homo sapiens 42-49 7012140-14 1981 We now report that the direct addition of insulin to particulate preparations containing high affinity insulin receptors and ribosomes derived from insulin-sensitive cells (not previously exposed to insulin) stimulates incorporation of 32P from [gamma-32P]ATP into ribosomal protein S6 1.5- to 3.0-fold. Phosphorus-32 236-239 insulin Homo sapiens 103-110 7012140-14 1981 We now report that the direct addition of insulin to particulate preparations containing high affinity insulin receptors and ribosomes derived from insulin-sensitive cells (not previously exposed to insulin) stimulates incorporation of 32P from [gamma-32P]ATP into ribosomal protein S6 1.5- to 3.0-fold. Phosphorus-32 236-239 insulin Homo sapiens 103-110 7012140-14 1981 We now report that the direct addition of insulin to particulate preparations containing high affinity insulin receptors and ribosomes derived from insulin-sensitive cells (not previously exposed to insulin) stimulates incorporation of 32P from [gamma-32P]ATP into ribosomal protein S6 1.5- to 3.0-fold. Phosphorus-32 236-239 insulin Homo sapiens 103-110 7012140-14 1981 We now report that the direct addition of insulin to particulate preparations containing high affinity insulin receptors and ribosomes derived from insulin-sensitive cells (not previously exposed to insulin) stimulates incorporation of 32P from [gamma-32P]ATP into ribosomal protein S6 1.5- to 3.0-fold. Phosphorus-32 252-255 insulin Homo sapiens 42-49 7012140-14 1981 We now report that the direct addition of insulin to particulate preparations containing high affinity insulin receptors and ribosomes derived from insulin-sensitive cells (not previously exposed to insulin) stimulates incorporation of 32P from [gamma-32P]ATP into ribosomal protein S6 1.5- to 3.0-fold. Phosphorus-32 252-255 insulin Homo sapiens 103-110 7012140-14 1981 We now report that the direct addition of insulin to particulate preparations containing high affinity insulin receptors and ribosomes derived from insulin-sensitive cells (not previously exposed to insulin) stimulates incorporation of 32P from [gamma-32P]ATP into ribosomal protein S6 1.5- to 3.0-fold. Phosphorus-32 252-255 insulin Homo sapiens 103-110 7012140-14 1981 We now report that the direct addition of insulin to particulate preparations containing high affinity insulin receptors and ribosomes derived from insulin-sensitive cells (not previously exposed to insulin) stimulates incorporation of 32P from [gamma-32P]ATP into ribosomal protein S6 1.5- to 3.0-fold. Phosphorus-32 252-255 insulin Homo sapiens 103-110 313567-1 1979 A protein of molecular weight 31,000 became labeled with 32P within 5 min after addition of insulin to differentiated 3T3-L1 preadipocytes previously incubated for 55 min with 32Pi. Phosphorus-32 57-60 insulin Homo sapiens 92-99 313567-3 1979 Incorporation of 32P into this protein was more than 20-fold greater in insulin-treated cells than in cells not exposed to the hormone. Phosphorus-32 17-20 insulin Homo sapiens 72-79 313567-6 1979 Incorporation of 32P into S6 could be detected within the same time period (5 min) and at the same insulin concentrations (0.1-1.0 nM) as are required to stimulate hexose uptake in both 3T3-L1 cells and mature mammalian adipocytes. Phosphorus-32 17-20 insulin Homo sapiens 99-106 176155-10 1976 Nevertheless, persistence of insulin-stimulated phosphorylation of the 123,000 peptide in the presence of epinephrine was shown by a 32P content of this peptide that was greater in the presence of both hormones than with either individually. Phosphorus-32 133-136 insulin Homo sapiens 29-36 176155-7 1976 When present as the sole hormone, insulin (100 microunits/ml) consistently and selectively stimulated the 32P incorporation into a peptide of molecular weight 123,000 (endoplasmic reticulum, cytoplasm) without significant alteration in the 32P content of any other major peptide. Phosphorus-32 240-243 insulin Homo sapiens 34-41 9527493-8 1997 In an attempt to resolve insulin-regulatable phosphoproteins, we subjected 32P-labeled subcellular fractions to two-dimensional gel electrophoresis (2-DE). Phosphorus-32 75-78 insulin Homo sapiens 25-32 9636226-4 1998 Insulin also increased by severalfold the 32P content of mTOR that was determined after purifying the protein from 32P-labeled adipocytes with rapamycin.FKBP12 agarose beads. Phosphorus-32 42-45 insulin Homo sapiens 0-7 9636226-4 1998 Insulin also increased by severalfold the 32P content of mTOR that was determined after purifying the protein from 32P-labeled adipocytes with rapamycin.FKBP12 agarose beads. Phosphorus-32 115-118 insulin Homo sapiens 0-7 8263034-7 1993 In the rat membranes, 1-100 nM glucagon (used as a positive control) stimulated [32P]GDP release by about 17% (P < .05); similarly, 0.1-100 nM insulin stimulated [32P]GDP release by 10-13% (P < .05). Phosphorus-32 166-169 insulin Homo sapiens 146-153 8636149-5 1996 Despite these defects of kinase activity, anti-phosphotyrosine immunoblotting of whole cell lysates and anti-phosphotyrosine immunoprecipitation of 32P-labeled cells showed insulin-stimulated tyrosine phosphorylation of a protein of approximately 185 kDa to an extent comparable to that seen in CHO cells expressing wild-type human insulin receptors. Phosphorus-32 148-151 insulin Homo sapiens 332-339 7926350-6 1994 On the other hand, in platelets incubated with [32P]orthophosphate, thrombin-induced incorporation of 32P radioactivity into phosphatidic acid (PA) was significantly lower in the sulphonylurea and insulin groups than in the diet group. Phosphorus-32 48-51 insulin Homo sapiens 197-204 8200291-6 1994 Insulin-stimulated 32P-incorporation into the insulin receptor beta-subunit was increased by 133% in the LGA group versus the control, whereas incorporation in the AGA group was equivalent to the control. Phosphorus-32 19-22 insulin Homo sapiens 0-7 8200291-6 1994 Insulin-stimulated 32P-incorporation into the insulin receptor beta-subunit was increased by 133% in the LGA group versus the control, whereas incorporation in the AGA group was equivalent to the control. Phosphorus-32 19-22 insulin Homo sapiens 46-53 7635975-3 1995 Approximately 50% of PCOS women (PCOS-Ser) had a significant increase in insulin-independent beta-subunit [32P]phosphate incorporation (3.7-fold, P < 0.05 vs other groups) in skin fibroblast insulin receptors that was present in serine residues while insulin-induced tyrosine phosphorylation was decreased (both P < 0.05 vs other groups). Phosphorus-32 107-110 insulin Homo sapiens 73-80 7635975-3 1995 Approximately 50% of PCOS women (PCOS-Ser) had a significant increase in insulin-independent beta-subunit [32P]phosphate incorporation (3.7-fold, P < 0.05 vs other groups) in skin fibroblast insulin receptors that was present in serine residues while insulin-induced tyrosine phosphorylation was decreased (both P < 0.05 vs other groups). Phosphorus-32 107-110 insulin Homo sapiens 194-201 7635975-3 1995 Approximately 50% of PCOS women (PCOS-Ser) had a significant increase in insulin-independent beta-subunit [32P]phosphate incorporation (3.7-fold, P < 0.05 vs other groups) in skin fibroblast insulin receptors that was present in serine residues while insulin-induced tyrosine phosphorylation was decreased (both P < 0.05 vs other groups). Phosphorus-32 107-110 insulin Homo sapiens 194-201 8263034-8 1993 In the human membranes, 10 pM to 100 nM insulin stimulated [32P]GDP release by 7-10%. Phosphorus-32 60-63 insulin Homo sapiens 40-47 8263034-9 1993 In the rat membranes, 10 nM insulin stimulated [32P]GDP release by 17 and 24% at 2 and 4 min, respectively (P < .05); in the human membranes, 10 nM insulin stimulated [32P]GDP release by about 9% at 2 and 4 min. Phosphorus-32 48-51 insulin Homo sapiens 28-35 8263034-9 1993 In the rat membranes, 10 nM insulin stimulated [32P]GDP release by 17 and 24% at 2 and 4 min, respectively (P < .05); in the human membranes, 10 nM insulin stimulated [32P]GDP release by about 9% at 2 and 4 min. Phosphorus-32 48-51 insulin Homo sapiens 151-158 8263034-9 1993 In the rat membranes, 10 nM insulin stimulated [32P]GDP release by 17 and 24% at 2 and 4 min, respectively (P < .05); in the human membranes, 10 nM insulin stimulated [32P]GDP release by about 9% at 2 and 4 min. Phosphorus-32 171-174 insulin Homo sapiens 28-35 8263034-9 1993 In the rat membranes, 10 nM insulin stimulated [32P]GDP release by 17 and 24% at 2 and 4 min, respectively (P < .05); in the human membranes, 10 nM insulin stimulated [32P]GDP release by about 9% at 2 and 4 min. Phosphorus-32 171-174 insulin Homo sapiens 151-158 8393956-5 1993 As compared with control subjects (2,690 +/- 637 fmol 32P incorporated), insulin (100 nmol/L)-stimulated tyrosine kinase activity was lower in NIDDM patients (1,262 +/- 318, P < .05), but not in obese subjects (2,640 +/- 731). Phosphorus-32 54-57 insulin Homo sapiens 73-80 1374639-4 1992 When 32P incorporation in beta-subunits of equal amounts of isolated HIR-A and HIR-B was measured, an increased 32P incorporation in tyrosine residues of the beta-subunit of HIR-B (2.5-fold) compared to that of HIR-A was found after in vitro insulin stimulation. Phosphorus-32 5-8 insulin Homo sapiens 242-249 8386623-3 1993 The incorporation of lectin-purified insulin receptors was assessed by cosedimentation of 125I-insulin binding and [32P]phospholipids in a sucrose gradient. Phosphorus-32 116-119 insulin Homo sapiens 37-44 1640858-9 1992 Autophosphorylation resulted in decreased 32P incorporation into proreceptors of cells transfected with mutated cDNA at both basal and insulin-stimulated states, without a change in insulin sensitivity. Phosphorus-32 42-45 insulin Homo sapiens 135-142 1374639-4 1992 When 32P incorporation in beta-subunits of equal amounts of isolated HIR-A and HIR-B was measured, an increased 32P incorporation in tyrosine residues of the beta-subunit of HIR-B (2.5-fold) compared to that of HIR-A was found after in vitro insulin stimulation. Phosphorus-32 112-115 insulin Homo sapiens 242-249 1650954-4 1991 In pulse-chase experiments, insulin stimulated depletion of 32P-labeled phosphoinositides only at 15 s. On the other hand, insulin treatment caused a biphasic diacyglycerol (DAG) production. Phosphorus-32 60-63 insulin Homo sapiens 28-35 1318189-7 1992 Added insulin increased the incorporation of 32P into phosphatidate in a dose-dependent manner that reached a steady state at 2 nM. Phosphorus-32 45-48 insulin Homo sapiens 6-13 1650954-4 1991 In pulse-chase experiments, insulin stimulated depletion of 32P-labeled phosphoinositides only at 15 s. On the other hand, insulin treatment caused a biphasic diacyglycerol (DAG) production. Phosphorus-32 60-63 insulin Homo sapiens 123-130 1846534-4 1991 We found that insulin stimulates 32P incorporation into PIP through both HIR-A and HIR-B to a similar extent (approx. Phosphorus-32 33-36 insulin Homo sapiens 14-21 2110001-3 1990 Alternatively, insulin receptors affinity purified from human term placenta were phosphorylated by protein kinase C prior to trypsin digestion of the 32P-labeled beta subunit. Phosphorus-32 150-153 insulin Homo sapiens 15-22 2515069-5 1989 Insulin stimulated [32P]phosphate incorporation into the 45 kDa protein approximately 2-fold. Phosphorus-32 20-23 insulin Homo sapiens 0-7 2478121-2 1989 PM1-mediated immunoprecipitation from hepatocyte extracts showed that insulin treatment of intact 32P-labelled hepatocytes caused the rapid phosphorylation of the peripheral-plasma-membrane cyclic AMP phosphodiesterase. Phosphorus-32 98-101 insulin Homo sapiens 70-77 2480780-7 1989 Addition of insulin further increased incorporation of 32P into calmodulin. Phosphorus-32 55-58 insulin Homo sapiens 12-19 2504716-9 1989 Phosphoamino acid analysis demonstrated that the phosphoserine/phosphothreonine content of in vivo 32P-labeled insulin receptors increased markedly within a 1-h exposure to insulin in vivo, whereas insulin-induced receptor desensitization was not apparent until 10-24 h after exposure to insulin. Phosphorus-32 99-102 insulin Homo sapiens 111-118 2504716-9 1989 Phosphoamino acid analysis demonstrated that the phosphoserine/phosphothreonine content of in vivo 32P-labeled insulin receptors increased markedly within a 1-h exposure to insulin in vivo, whereas insulin-induced receptor desensitization was not apparent until 10-24 h after exposure to insulin. Phosphorus-32 99-102 insulin Homo sapiens 173-180 2504716-9 1989 Phosphoamino acid analysis demonstrated that the phosphoserine/phosphothreonine content of in vivo 32P-labeled insulin receptors increased markedly within a 1-h exposure to insulin in vivo, whereas insulin-induced receptor desensitization was not apparent until 10-24 h after exposure to insulin. Phosphorus-32 99-102 insulin Homo sapiens 173-180 2504716-9 1989 Phosphoamino acid analysis demonstrated that the phosphoserine/phosphothreonine content of in vivo 32P-labeled insulin receptors increased markedly within a 1-h exposure to insulin in vivo, whereas insulin-induced receptor desensitization was not apparent until 10-24 h after exposure to insulin. Phosphorus-32 99-102 insulin Homo sapiens 173-180 2546561-4 1989 In contrast, the dimer only partially (23%) mimicked insulin"s effect on phosphate incorporation into insulin receptors immunoprecipitated after equilibration of cells with [32P]phosphate. Phosphorus-32 174-177 insulin Homo sapiens 53-60 2546561-4 1989 In contrast, the dimer only partially (23%) mimicked insulin"s effect on phosphate incorporation into insulin receptors immunoprecipitated after equilibration of cells with [32P]phosphate. Phosphorus-32 174-177 insulin Homo sapiens 102-109 3166375-4 1988 The 32P-labelled insulin-receptor beta-subunits were then isolated, cleaved with trypsin followed by protease V8 and the [32P]phosphopeptides generated were analysed by thin layer electrophoresis and chromatography. Phosphorus-32 4-7 insulin Homo sapiens 17-24 2649086-8 1989 Increased incorporation of 32P in these experiments implies decreased phosphorylation in situ when tissues were incubated with insulin and leucine. Phosphorus-32 27-30 insulin Homo sapiens 127-134 2649086-10 1989 In the presence of leucine, however, incorporation of 32P into BCDH was markedly increased, and insulin increased 32P incorporation still further. Phosphorus-32 114-117 insulin Homo sapiens 96-103 3066355-9 1988 Analysis of immunoprecipitated HLA molecules by two-dimensional gel electrophoresis showed that TPA and insulin stimulated the incorporation of 32P into different 45 kDa molecular species, suggesting that different sites were phosphorylated by two agents. Phosphorus-32 144-147 insulin Homo sapiens 104-111 2900139-12 1988 None of these correspond to the peptides whose 32P-labelling increase in response to insulin or TPA. Phosphorus-32 47-50 insulin Homo sapiens 85-92 2900140-3 1988 Two tryptic peptides derived from the enzyme become more radioactive after treatment of 32P-labelled cells with insulin. Phosphorus-32 88-91 insulin Homo sapiens 112-119 2900140-12 1988 On stimulation with insulin, phosphorylation appeared to occur primarily at site 6, thus accounting for the increase in 32P-labelling of T4a. Phosphorus-32 120-123 insulin Homo sapiens 20-27 2662545-2 1989 In the case of insulin-treated plasma membranes the amount of incorporated 32P is more than 4 times higher than that of the basal level. Phosphorus-32 75-78 insulin Homo sapiens 15-22 3286642-3 1988 Nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis of 125I-insulin affinity cross-linked and 32P-autophosphorylated alpha beta heterodimers demonstrated that the insulin-dependent reassociation to the alpha 2 beta 2 heterotetrameric state occurred both covalently and noncovalently under these conditions. Phosphorus-32 112-115 insulin Homo sapiens 181-188 3286642-7 1988 However, 4 h of insulin pretreatment of the alpha beta heterodimer preparation induced the formation (6-fold) of a covalent 32P-labeled alpha 2 beta 2 heterotetrameric complex. Phosphorus-32 124-127 insulin Homo sapiens 16-23 2832399-2 1988 Autophosphorylation in the presence of insulin is a highly concerted reaction; tryptic digestion of insulin receptor beta subunits derived from preparations whose kinase activation ranges from under 5% to 100% of maximal yields the same array of [32P]Tyr(P)-containing peptides over the entire range. Phosphorus-32 247-250 insulin Homo sapiens 39-46 3283160-4 1988 Insulin gene expression was quantified by measuring insulin mRNA by blot hybridization analysis using a [32P] cDNA probe encoding human insulin. Phosphorus-32 105-108 insulin Homo sapiens 0-7 3283160-4 1988 Insulin gene expression was quantified by measuring insulin mRNA by blot hybridization analysis using a [32P] cDNA probe encoding human insulin. Phosphorus-32 105-108 insulin Homo sapiens 136-143 2832399-2 1988 Autophosphorylation in the presence of insulin is a highly concerted reaction; tryptic digestion of insulin receptor beta subunits derived from preparations whose kinase activation ranges from under 5% to 100% of maximal yields the same array of [32P]Tyr(P)-containing peptides over the entire range. Phosphorus-32 247-250 insulin Homo sapiens 100-107 2832399-8 1988 Rather, insulin directs 32P incorporation preferentially into those domains most productive of kinase activation. Phosphorus-32 24-27 insulin Homo sapiens 8-15 2821993-9 1987 Insulin increased 32P incorporation into the 180 kDa band 2.7-fold (S.E.M. Phosphorus-32 18-21 insulin Homo sapiens 0-7 3279949-7 1988 However, insulin stimulated autophosphorylation per receptor was different being greatest (p less than 0.05) in muscle (334 +/- 104 32P cpm) and similar in adipose tissue (114 +/- 10) and liver (183 +/- 68). Phosphorus-32 132-135 insulin Homo sapiens 9-16 3556284-3 1987 HIT cells were loaded with 32P and stimulated with either 40 mM K+ or 19.4 mM glucose, both of which trigger the immediate release of insulin. Phosphorus-32 27-30 insulin Homo sapiens 134-141 3540953-8 1987 Insulin (0.5 nM, 100 nM) stimulated within 2 min the 32P incorporation into a 116-kDa band, a 62-kDa band, and three bands between 45 kDa and 50 kDa 2- to 10-fold. Phosphorus-32 53-56 insulin Homo sapiens 0-7 3032719-4 1987 Insulin stimulated 32P-incorporation into the beta-subunit of the insulin receptor of phorbolester or isoprenaline treated cells was reduced to 20-60% of the values found with receptor from control cells at insulin concentrations between 10(-10) mol/l and 10(-7) mol/l. Phosphorus-32 19-22 insulin Homo sapiens 0-7 3032719-4 1987 Insulin stimulated 32P-incorporation into the beta-subunit of the insulin receptor of phorbolester or isoprenaline treated cells was reduced to 20-60% of the values found with receptor from control cells at insulin concentrations between 10(-10) mol/l and 10(-7) mol/l. Phosphorus-32 19-22 insulin Homo sapiens 66-73 3032719-4 1987 Insulin stimulated 32P-incorporation into the beta-subunit of the insulin receptor of phorbolester or isoprenaline treated cells was reduced to 20-60% of the values found with receptor from control cells at insulin concentrations between 10(-10) mol/l and 10(-7) mol/l. Phosphorus-32 19-22 insulin Homo sapiens 207-214 2582429-5 1985 We report here that placental polyadenylylated RNAs from the first and third trimester of normal pregnancy as well as from term pregnancies of diabetic mothers hybridize to a 32P-labeled cloned cDNA of an insulin-related sequence expressed in fetal pancreas. Phosphorus-32 175-178 insulin Homo sapiens 205-212 2881538-3 1986 Experiments with 32P-labelled adipocytes showed that insulin increased the total phosphorylation of acetyl-CoA carboxylase from 2.7 to 3.5 molecules of phosphate/240 kDa subunit, and confirmed that this increase was partially accounted for by phosphorylation within a specific peptide (the "I-site" peptide). Phosphorus-32 17-20 insulin Homo sapiens 53-60 3733682-5 1986 The insulin receptor was then isolated from 32P-labeled IM-9 cells that had been exposed to insulin. Phosphorus-32 44-47 insulin Homo sapiens 4-11 2419331-2 1986 8-Bromo-cAMP (1 mM) or forskolin (10 microM) enhanced the phosphorylation of the insulin receptor purified from 32P-labeled cells by affinity chromatography on wheat germ agglutinin-agarose and immunoprecipitation with monoclonal antibody. Phosphorus-32 112-115 insulin Homo sapiens 81-88 3001475-5 1986 DNA was extracted from leukocytes and after digestion with Sst 1, and electrophoresis, the DNA was blotted to nitrocellulose filters and hybridized to a alpha 32P-labeled insulin gene probe. Phosphorus-32 159-162 insulin Homo sapiens 171-178 3528154-7 1986 Upon the addition of insulin, [32P]orthophosphate incorporated into the beta-subunit increased 4.5-fold (7-fold with respect to [32P]tyrosine) and was complete within 1 min (t1/2 = 8 s). Phosphorus-32 31-34 insulin Homo sapiens 21-28 2940115-8 1986 In the absence of insulin trypsin treatment yielded eight [32P]phosphopeptides, two of which coincided with the ones due to protein kinase C. Insulin led to the appearance of three new [32P]phosphopeptides. Phosphorus-32 186-189 insulin Homo sapiens 142-149 2997784-5 1985 Addition of insulin to labeled adipocytes did not change the specific activity of the gamma-phosphate of ATP but produced a specific and sharp decrease in the 32P-phosphate content of IGF-II receptors in the plasma membrane. Phosphorus-32 159-162 insulin Homo sapiens 12-19 2997784-7 1985 The insulin-mediated decrease in the [32P]phosphate content of IGF-II receptors from the plasma membrane was rapid in onset, paralleled the increase in the number of IGF-II receptors on the cell surface, and persisted for at least 30 min in the presence of insulin. Phosphorus-32 38-41 insulin Homo sapiens 4-11 2997784-7 1985 The insulin-mediated decrease in the [32P]phosphate content of IGF-II receptors from the plasma membrane was rapid in onset, paralleled the increase in the number of IGF-II receptors on the cell surface, and persisted for at least 30 min in the presence of insulin. Phosphorus-32 38-41 insulin Homo sapiens 257-264 2993346-9 1985 When insulin receptors from stroma were extracted with Triton X-100 and incubated with [gamma-32P]ATP and Mn, insulin increased the incorporation of 32P into the beta-subunit of the receptor 5-fold. Phosphorus-32 94-97 insulin Homo sapiens 5-12 2993346-9 1985 When insulin receptors from stroma were extracted with Triton X-100 and incubated with [gamma-32P]ATP and Mn, insulin increased the incorporation of 32P into the beta-subunit of the receptor 5-fold. Phosphorus-32 94-97 insulin Homo sapiens 110-117 6309826-2 1983 This purified insulin receptor kinase specifically catalyzed the incorporation of 32P from [gamma-32P]ATP into not only the beta-subunit of the insulin receptor but also histone H2B, a synthetic peptide which is sequentially similar to the site of tyrosine phosphorylation in pp60src (a gene product of the Rous sarcoma virus) and antibodies to pp60src present in the sera obtained from three rabbits bearing tumors induced by the Rous sarcoma virus. Phosphorus-32 82-85 insulin Homo sapiens 14-21 6384712-1 1984 Insulin action on [32P]-phosphate incorporation into brain membranes was determined. Phosphorus-32 19-22 insulin Homo sapiens 0-7 6325418-14 1984 Under these conditions, the estimated turnover number of the kinase ranges between 30 and 100 pmol of 32P transferred per min/pmol of insulin bound. Phosphorus-32 102-105 insulin Homo sapiens 134-141 6358209-7 1983 Porcine insulin stimulated 4- to 5-fold the incorporation of 32P in a protein of Mr = 95,000, corresponding to the beta-subunit of the insulin receptor. Phosphorus-32 61-64 insulin Homo sapiens 8-15 6358209-7 1983 Porcine insulin stimulated 4- to 5-fold the incorporation of 32P in a protein of Mr = 95,000, corresponding to the beta-subunit of the insulin receptor. Phosphorus-32 61-64 insulin Homo sapiens 135-142 2981245-2 1985 In studies with cell lines derived from six normal subjects, insulin (10(-7) M) caused an average increase of approximately 200% in 32P incorporation into the 95K subunit of the insulin receptor. Phosphorus-32 132-135 insulin Homo sapiens 61-68 2981245-2 1985 In studies with cell lines derived from six normal subjects, insulin (10(-7) M) caused an average increase of approximately 200% in 32P incorporation into the 95K subunit of the insulin receptor. Phosphorus-32 132-135 insulin Homo sapiens 178-185 6224483-5 1983 Islets prelabelled with [32P]Pi and incubated with 28 mM-glucose secreted significantly more insulin and had greater incorporation of radioactivity into the 54 kDa protein than did islets incubated under basal conditions in the presence of 5 mM-glucose. Phosphorus-32 25-28 insulin Homo sapiens 93-100