PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 18570467-7 2008 However, the rupture of the Gly( P 1) approximately Ile( P 1") amide bond is destabilized in the static QM/MM calculations, owing to the positioning of the Ile( P 1") side chain inside the MMP-2 S 1" pocket and to the inability of simple energy miminization methodologies to properly relax complex systems. Isoleucine 52-55 matrix metallopeptidase 2 Homo sapiens 189-194 7890717-6 1995 MMP-2 cleaves at the same Gly-Ile/Leu bond in the collagen alpha chains as interstitial collagenases with kcat and Km values similar to that of MMP-1. Isoleucine 30-33 matrix metallopeptidase 2 Homo sapiens 0-5 29989088-8 2018 We herein report 4 novel inhibitor candidates of Asp-Ile-Phe, Asp-Ile-Tyr, Asp-Ile-Lys and Hser-Gly-Phe with high potency and selectivity binding to MMP-2, as well as 6 novel inhibitor candidates of Chg-Ile-Ile, Chg-Ile-Leu, Chg-Ile-Glu, Chg-Ile-Met, Chg-Val-Ile and Chg-Val-Leu selectively binding to MMP-7. Isoleucine 53-56 matrix metallopeptidase 2 Homo sapiens 149-154 25375834-7 2014 Similarly, a natural substrate of MMP-2, Ace-Gln-Gly ~ Ile-Ala-Gly-Nme, can be converted to an inhibiting compound by two replacements, Ile by Cys and Gly by the d isomer of Cys, favoring formation of the zinc finger motif. Isoleucine 55-58 matrix metallopeptidase 2 Homo sapiens 34-39 25375834-7 2014 Similarly, a natural substrate of MMP-2, Ace-Gln-Gly ~ Ile-Ala-Gly-Nme, can be converted to an inhibiting compound by two replacements, Ile by Cys and Gly by the d isomer of Cys, favoring formation of the zinc finger motif. Isoleucine 136-139 matrix metallopeptidase 2 Homo sapiens 34-39 18570467-7 2008 However, the rupture of the Gly( P 1) approximately Ile( P 1") amide bond is destabilized in the static QM/MM calculations, owing to the positioning of the Ile( P 1") side chain inside the MMP-2 S 1" pocket and to the inability of simple energy miminization methodologies to properly relax complex systems. Isoleucine 156-159 matrix metallopeptidase 2 Homo sapiens 189-194 10559137-3 1999 The amino acid sequences in interstitial collagen (Gly-Leu/Ile) and laminin-5 (Ala-Leu) that are cleaved by MMP-2 are homologous to a region (Gly(32)-Leu(33)) within human big endothelin-1[1 to 38] (big ET-1). Isoleucine 59-62 matrix metallopeptidase 2 Homo sapiens 108-113 10976799-7 2000 MMP-2 (Mr 72 000 type IV collagenase; gelatinase A) was found to cleave the substrates at two sites, a Gly-Ile bond and a Gly-Gln bond. Isoleucine 107-110 matrix metallopeptidase 2 Homo sapiens 0-5 20641641-17 2004 A peptide, GGPRQITAG, was found to be a MMP-2/9 substrate from a phage library and is cleaved between Gln (Q) and Ile (I) residues (14). Isoleucine 114-117 matrix metallopeptidase 2 Homo sapiens 40-47 20641641-21 2004 The NIR fluorescence signal will increase when the Gln-Ile bond is cleaved by MMP-2/9, releasing fragments that contain Cy5.5. Isoleucine 55-58 matrix metallopeptidase 2 Homo sapiens 78-85