PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22898766-6 2012 RESULTS: Neprilysin prevented IAPP fibrillisation by cleaving IAPP at Arg(11)-Leu(12), Leu(12)-Ala(13), Asn(14)-Phe(15), Phe(15)-Leu(16), Asn(22)-Phe(23) and Ala(25)-Ile(26). Leucine 78-81 membrane metalloendopeptidase Homo sapiens 9-19 22898766-6 2012 RESULTS: Neprilysin prevented IAPP fibrillisation by cleaving IAPP at Arg(11)-Leu(12), Leu(12)-Ala(13), Asn(14)-Phe(15), Phe(15)-Leu(16), Asn(22)-Phe(23) and Ala(25)-Ile(26). Leucine 87-90 membrane metalloendopeptidase Homo sapiens 9-19 22898766-6 2012 RESULTS: Neprilysin prevented IAPP fibrillisation by cleaving IAPP at Arg(11)-Leu(12), Leu(12)-Ala(13), Asn(14)-Phe(15), Phe(15)-Leu(16), Asn(22)-Phe(23) and Ala(25)-Ile(26). Leucine 87-90 membrane metalloendopeptidase Homo sapiens 9-19 9218437-5 1997 The predominant amino acids detected by protein sequence analysis following cleavage of insoluble elastin with HME, MME, and 92-kDa gelatinase were Leu, Ile, Ala, Gly, and Val. Leucine 148-151 membrane metalloendopeptidase Homo sapiens 116-119 18753140-5 2008 Like Motif-1 binding, the CD44 beta strand binds the shallow groove between strand beta5C and helix alpha1C and augments the beta sheet beta5C-beta7C from subdomain C. Two hydrophobic CD44 residues, Leu and Ile, are docked into a hydrophobic pocket with the formation of hydrogen bonds between Asn of the CD44 short loop and loop beta4C-beta5C from subdomain C. This binding mode resembles that of NEP (neutral endopeptidase 24.11) rather than ICAM-2. Leucine 199-202 membrane metalloendopeptidase Homo sapiens 398-401 18753140-5 2008 Like Motif-1 binding, the CD44 beta strand binds the shallow groove between strand beta5C and helix alpha1C and augments the beta sheet beta5C-beta7C from subdomain C. Two hydrophobic CD44 residues, Leu and Ile, are docked into a hydrophobic pocket with the formation of hydrogen bonds between Asn of the CD44 short loop and loop beta4C-beta5C from subdomain C. This binding mode resembles that of NEP (neutral endopeptidase 24.11) rather than ICAM-2. Leucine 199-202 membrane metalloendopeptidase Homo sapiens 403-430 15134871-5 2004 NEP cleaved substance P (SP) at Gln(6)-Phe(7), Phe(7)[see text]-Phe(8), and Gly(9)-Leu(10) and neurotensin (NT) at Pro(10)-Tyr(11) and Tyr(11)-Ile(12). Leucine 83-86 membrane metalloendopeptidase Homo sapiens 0-3 9218437-6 1997 HME and MME were similar in their substrate specificity and showed a stronger preference for Leu/Ile than did the 92-kDa enzyme. Leucine 93-96 membrane metalloendopeptidase Homo sapiens 8-11 3909153-9 1985 Kinetic studies with pure human renal NEP showed that the chemotactic peptide fMet-Leu-Phe was one of the best biologically active substrates (Km, 59 X 10(-6) M; kcat, 3654 min-1). Leucine 83-86 membrane metalloendopeptidase Homo sapiens 38-41 1935939-5 1991 By using inhibitors of distinct classes of endoproteases, this particular fMet-Leu-Phe degradation was attributed exclusively to an exoplasmic metalloendoprotease that matches the ubiquitous neutral endopeptidase (NEP). Leucine 79-82 membrane metalloendopeptidase Homo sapiens 191-212 1935939-5 1991 By using inhibitors of distinct classes of endoproteases, this particular fMet-Leu-Phe degradation was attributed exclusively to an exoplasmic metalloendoprotease that matches the ubiquitous neutral endopeptidase (NEP). Leucine 79-82 membrane metalloendopeptidase Homo sapiens 214-217 1935939-9 1991 Based on these and previously reported results, a novel model is proposed in which the fMet-Leu-Phe-induced inflammatory stimulation of PMN involves both NEP and the fMet-Leu-Phe receptor. Leucine 92-95 membrane metalloendopeptidase Homo sapiens 154-157 8587470-5 1995 Interchange between Leu and Trp abolished the inhibitory activities for ECE and NEP, but the compound remained active for ACE. Leucine 20-23 membrane metalloendopeptidase Homo sapiens 80-83 2145213-2 1990 The concentration of NEP was quantified in detergent extracts of synovial tissues by the percentage hydrolysis of [3H-D-Ala]-Leu enkephalin/hr/100 mg of tissue. Leucine 125-128 membrane metalloendopeptidase Homo sapiens 21-24 3288636-9 1988 First, we confirm that NEP present on the plasma membrane cleaves fMLP at the Met-Leu bond; then the dipeptide Leu-Phe is cleaved by a dipeptidase. Leucine 82-85 membrane metalloendopeptidase Homo sapiens 23-26 3288636-9 1988 First, we confirm that NEP present on the plasma membrane cleaves fMLP at the Met-Leu bond; then the dipeptide Leu-Phe is cleaved by a dipeptidase. Leucine 111-114 membrane metalloendopeptidase Homo sapiens 23-26