PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1660880-5 1991 To our surprise, the distal Leu mutant has a less restricted, less sterically crowded distal heme pocket than that of the distal Val mutant myoglobin, despite the fact that Leu has a larger side chain volume than Val. Leucine 28-31 myoglobin Homo sapiens 140-149 10529220-8 1999 268, 6995-7010] that a mutation at position 29 (B10, helix notation), e.g. , Leu --> Phe, can inhibit the autoxidation of the heme iron of myoglobin. Leucine 77-80 myoglobin Homo sapiens 142-151 8342560-5 1993 The replacement of phenylalanine G5, which is localized within the heme pocket, by a leucine abolishes several contacts between the heme and the globin and leads to an environment of the heme having some similarities with that observed in myoglobin. Leucine 85-92 myoglobin Homo sapiens 239-248 1429633-1 1992 Recombinant human myoglobin mutants with the distal His residue (E7, His64) replaced by Leu, Val, or Gln residues were prepared by site-directed mutagenesis and expression in Escherichia coli. Leucine 88-91 myoglobin Homo sapiens 18-27 1429633-3 1992 Mutations, His-->Val and His-->Leu, remove the heme-bound water molecule resulting in a five-coordinate heme iron at neutral pH, while the heme-bound water molecule appears to be retained in the engineered myoglobin with His-->Gln substitution as in the wild-type protein. Leucine 37-40 myoglobin Homo sapiens 212-221 1660880-1 1991 Recombinant human myoglobin mutants with the distal histidine residue replaced by Leu, Val, or Gln residues have been prepared by site-directed mutagenesis and expression in Escherichia coli. Leucine 82-85 myoglobin Homo sapiens 18-27 9374489-0 1997 The effects of heme pocket hydrophobicity on the ligand binding dynamics in myoglobin as studied with leucine 29 mutants. Leucine 102-109 myoglobin Homo sapiens 76-85 9083641-5 1997 Large apolar residues (Leu, Phe, Trp) at the B10 and E11 positions inhibit NO-induced and autooxidation in both myoglobin and hemoglobin by excluding oxidants and proton donors from the immediate vicinity of the bound ligand. Leucine 23-26 myoglobin Homo sapiens 112-121 1660880-5 1991 To our surprise, the distal Leu mutant has a less restricted, less sterically crowded distal heme pocket than that of the distal Val mutant myoglobin, despite the fact that Leu has a larger side chain volume than Val. Leucine 173-176 myoglobin Homo sapiens 140-149 33703997-5 2022 Our data showed that 4 mM leucine significantly increased protein expression levels of slow MyHC, Myoglobin, Troponin I-SS, AdipoQ, AdipoR1, phospho-AMPK (p-AMPK) and PGC-1alpha and mRNA expression levels of AMPKalpha2, PGC-1alpha, AdipoQ and AdipoR1, and significantly decreased fast MyHC protein expression. Leucine 26-33 myoglobin Homo sapiens 98-107 34543141-2 2021 The experiment lasted for 42 d. The results showed that dietary supplementation of 0.25% leucine significantly increased the protein expressions of slow MyHC, myoglobin and Troponin I-SS and the mRNA expressions of MyHC I, MyHC IIa, Tnni1, Tnnc1, Tnnt1 and myoglobin, while decreased the protein level of fast MyHC and the mRNA level of MyHC IIb in longissimus dorsi (LD) muscle. Leucine 89-96 myoglobin Homo sapiens 159-168 34543141-2 2021 The experiment lasted for 42 d. The results showed that dietary supplementation of 0.25% leucine significantly increased the protein expressions of slow MyHC, myoglobin and Troponin I-SS and the mRNA expressions of MyHC I, MyHC IIa, Tnni1, Tnnc1, Tnnt1 and myoglobin, while decreased the protein level of fast MyHC and the mRNA level of MyHC IIb in longissimus dorsi (LD) muscle. Leucine 89-96 myoglobin Homo sapiens 257-266 32617526-6 2020 In addition, molecular dynamics modeling suggested that hydrophobic amino acid residues (Phe 111, Leu 10, Ala 115, Pro 116) in pepsin and polar amino acid residues (Tyr 146, Thr 95) in myoglobin were found in the proximity of binding sites, which could result in the low digestibility of myoglobin. Leucine 98-101 myoglobin Homo sapiens 185-194