Pub. Date : 2004
PMID : 22073424
9 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | For this, investigators developed gadolinium-bis-5-hydroxytriptamide-diethylenetriamine pentaacetic acid (Gd-bis-5-HT-DTPA; also known as MPO-Gd), a magnetic resonance imaging (MRI) agent, that acts as a substrate for the MPO and used it for the noninvasive visualization of MPO activity in normal and diseased tissues (3). | gd-bis-5-ht-dtpa | myeloperoxidase | Homo sapiens |
| 2 | For this, investigators developed gadolinium-bis-5-hydroxytriptamide-diethylenetriamine pentaacetic acid (Gd-bis-5-HT-DTPA; also known as MPO-Gd), a magnetic resonance imaging (MRI) agent, that acts as a substrate for the MPO and used it for the noninvasive visualization of MPO activity in normal and diseased tissues (3). | gd-bis-5-ht-dtpa | myeloperoxidase | Homo sapiens |
| 3 | For this, investigators developed gadolinium-bis-5-hydroxytriptamide-diethylenetriamine pentaacetic acid (Gd-bis-5-HT-DTPA; also known as MPO-Gd), a magnetic resonance imaging (MRI) agent, that acts as a substrate for the MPO and used it for the noninvasive visualization of MPO activity in normal and diseased tissues (3). | gd-bis-5-ht-dtpa | myeloperoxidase | Homo sapiens |
| 4 | Oxidative activation of the paramagnetic substrate (Gd-bis-5-HT-DTPA) by MPO leads to oligomerization and entrapment of the activated Gd-bis-5-HT-DTPA within the tissue by cross-linking the monomer or the oligomer with tyrosine-containing proteins, thereby increasing the localized concentration Gd at the site of MPO activity as explained in detail by Rodriguez et al. | gd-bis-5-ht-dtpa | myeloperoxidase | Homo sapiens |
| 5 | Oxidative activation of the paramagnetic substrate (Gd-bis-5-HT-DTPA) by MPO leads to oligomerization and entrapment of the activated Gd-bis-5-HT-DTPA within the tissue by cross-linking the monomer or the oligomer with tyrosine-containing proteins, thereby increasing the localized concentration Gd at the site of MPO activity as explained in detail by Rodriguez et al. | gd-bis-5-ht-dtpa | myeloperoxidase | Homo sapiens |
| 6 | Oxidative activation of the paramagnetic substrate (Gd-bis-5-HT-DTPA) by MPO leads to oligomerization and entrapment of the activated Gd-bis-5-HT-DTPA within the tissue by cross-linking the monomer or the oligomer with tyrosine-containing proteins, thereby increasing the localized concentration Gd at the site of MPO activity as explained in detail by Rodriguez et al. | gd-bis-5-ht-dtpa | myeloperoxidase | Homo sapiens |
| 7 | Oxidative activation of the paramagnetic substrate (Gd-bis-5-HT-DTPA) by MPO leads to oligomerization and entrapment of the activated Gd-bis-5-HT-DTPA within the tissue by cross-linking the monomer or the oligomer with tyrosine-containing proteins, thereby increasing the localized concentration Gd at the site of MPO activity as explained in detail by Rodriguez et al. | gd-bis-5-ht-dtpa | myeloperoxidase | Homo sapiens |
| 8 | In addition, the oligomeric and entrapped Gd-bis-5-HT-DTPA has a slow clearance rate from the tissue compared to the non-activated compound, and delayed clearance of the activated Gd-bis-5-HT-DTPA allows for the imaging of MPO in the inflamed tissue. | gd-bis-5-ht-dtpa | myeloperoxidase | Homo sapiens |
| 9 | In addition, the oligomeric and entrapped Gd-bis-5-HT-DTPA has a slow clearance rate from the tissue compared to the non-activated compound, and delayed clearance of the activated Gd-bis-5-HT-DTPA allows for the imaging of MPO in the inflamed tissue. | gd-bis-5-ht-dtpa | myeloperoxidase | Homo sapiens |