Comparison of Visual Fields: Humphrey Field Analyzer (HFA) SITA Strategy, SCOPE (GATE Strategy) and Humphrey MATRIX Perimeter
The purpose of this study is to compare three perimetric techniques regarding progression of the visual field.
Observational Model: Cohort, Time Perspective: Prospective
HFA, Octopus, MATRIX
Centre for Ophthalmology, Institute for Ophthalmic Research
University Hospital Tuebingen
Results (where available)
- Source: http://clinicaltrials.gov/show/NCT01068938
- Information obtained from ClinicalTrials.gov on July 15, 2010
Medical and Biotech [MESH] Definitions
Matrix Metalloproteinase 20
A secreted matrix metalloproteinase that is the predominant proteolytic activity in the enamel matrix. The enzyme has a high specificity for dental enamel matrix protein AMELOGENIN.
Matrix Metalloproteinase 16
A transmembrane domain-containing matrix metalloproteinase. It is synthesized as an inactive zymogen that is activated by the proteolytic action of PROPROTEIN CONVERTASES. Matrix metalloproteinase 16 plays a direct role in the cleavage of proteins in the pericellular environment. In addition it can function indirectly by enzymatically activating the proprotein form of other MATRIX METALLOPROTEINASES such as the zymogen of MATRIX METALLOPROTEINASE 2.
Matrix Metalloproteinase 11
A secreted matrix metalloproteinase that is believed to play a role in EXTRACELLULAR MATRIX remodeling and cell fate determination during normal and pathological processes. Matrix metalloproteinase 11 was originally isolated in primary BREAST NEOPLASMS and may be involved in the process of tumorigenesis.
Matrix Metalloproteinase 14
A transmembrane domain-containing matrix metalloproteinase. It is synthesized as an inactive zymogen that is activated by the action of PROPROTEIN CONVERTASES such as FURIN. Matrix metalloproteinase 14 plays a direct role in the cleavage of proteins in the pericellular environment. In addition it can function indirectly by enzymatically activating the proprotein form of MATRIX METALLOPROTEINASE 15.
Matrix Metalloproteinase 13
A secreted matrix metalloproteinase that plays a physiological role in the degradation of extracellular matrix found in skeletal tissues. It is synthesized as an inactive precursor that is activated by the proteolytic cleavage of its N-terminal propeptide.
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