All Relations between retina cone cell and matrix compartment

Publication Sentence Publish Date Extraction Date Species
H H Varner, M E Rayborn, A M Osterfeld, J G Hollyfiel. Localization of proteoglycan within the extracellular matrix sheath of cone photoreceptors. Experimental eye research. vol 44. issue 5. 1987-10-08. PMID:2442023. the size and appearance of the stained material are consistent with its being proteoglycan and its distribution is consistent with its being a component of the cone extracellular matrix sheath. 1987-10-08 2023-08-11 human
L V Johnson, G S Hagema. Enzymatic characterization of peanut agglutinin-binding components in the retinal interphotoreceptor matrix. Experimental eye research. vol 44. issue 4. 1987-08-17. PMID:3109930. the lectin peanut agglutinin (pna), which preferentially binds galactose-containing carbohydrates, especially galactose-galactosamine linkages, selectively labels cone photoreceptor-associated domains of the ipm ('cone matrix sheaths') in a variety of vertebrate retinas. 1987-08-17 2023-08-11 Not clear
L V Johnson, G S Hagema. Enzymatic characterization of peanut agglutinin-binding components in the retinal interphotoreceptor matrix. Experimental eye research. vol 44. issue 4. 1987-08-17. PMID:3109930. all proteolytic enzymes tested cause a marked reduction in pna-binding to cone matrix sheaths, suggesting that proteinaceous components are important to their organization. 1987-08-17 2023-08-11 Not clear
L V Johnson, G S Hagema. Enzymatic characterization of peanut agglutinin-binding components in the retinal interphotoreceptor matrix. Experimental eye research. vol 44. issue 4. 1987-08-17. PMID:3109930. exposure to o-glycanase, but not n-glycanase, markedly reduces binding of pna to cone matrix sheaths indicating that o-linked oligosaccharides are probably responsible for its binding. 1987-08-17 2023-08-11 Not clear
L V Johnson, G S Hagema. Enzymatic characterization of peanut agglutinin-binding components in the retinal interphotoreceptor matrix. Experimental eye research. vol 44. issue 4. 1987-08-17. PMID:3109930. exposure to chondroitinases causes disruption of the morphological integrity of cone matrix sheaths and slight diminution of pna binding. 1987-08-17 2023-08-11 Not clear
L V Johnson, G S Hagema. Enzymatic characterization of peanut agglutinin-binding components in the retinal interphotoreceptor matrix. Experimental eye research. vol 44. issue 4. 1987-08-17. PMID:3109930. taken together, these observations suggest that pna-binding to cone matrix sheaths is due to the presence of glycoconjugates with galactose-containing, o-linked oligosaccharide chains. 1987-08-17 2023-08-11 Not clear
G S Hageman, L V Johnso. Chondroitin 6-sulfate glycosaminoglycan is a major constituent of primate cone photoreceptor matrix sheaths. Current eye research. vol 6. issue 4. 1987-07-08. PMID:3107909. chondroitin 6-sulfate glycosaminoglycan is a major constituent of primate cone photoreceptor matrix sheaths. 1987-07-08 2023-08-11 Not clear
G S Hageman, L V Johnso. Chondroitin 6-sulfate glycosaminoglycan is a major constituent of primate cone photoreceptor matrix sheaths. Current eye research. vol 6. issue 4. 1987-07-08. PMID:3107909. recent work suggests that chemically and structurally distinct domains of the interphotoreceptor matrix ("cone matrix sheaths") surround cone photoreceptor outer segments and ellipsoids. 1987-07-08 2023-08-11 Not clear
G S Hageman, L V Johnso. Chondroitin 6-sulfate glycosaminoglycan is a major constituent of primate cone photoreceptor matrix sheaths. Current eye research. vol 6. issue 4. 1987-07-08. PMID:3107909. previous histochemical and biochemical investigations have shown that a variety of glycosaminoglycans are components of the interphotoreceptor matrix and that the structural integrity of cone sheaths is slightly disrupted by glycosaminoglycan-degrading enzymes. 1987-07-08 2023-08-11 Not clear
G S Hageman, L V Johnso. Chondroitin 6-sulfate glycosaminoglycan is a major constituent of primate cone photoreceptor matrix sheaths. Current eye research. vol 6. issue 4. 1987-07-08. PMID:3107909. in order to pursue the possibility that specific glycosaminoglycan species establish cone matrix sheath domains, monoclonal antibodies directed against various unsaturated glycosaminoglycans have been screened on sections of primate retina. 1987-07-08 2023-08-11 Not clear
G S Hageman, L V Johnso. Chondroitin 6-sulfate glycosaminoglycan is a major constituent of primate cone photoreceptor matrix sheaths. Current eye research. vol 6. issue 4. 1987-07-08. PMID:3107909. the results of these studies identify chondroitin 6-sulfate glycosaminoglycan as a specific component of primate cone matrix sheaths. 1987-07-08 2023-08-11 Not clear
G S Hageman, L V Johnso. Biochemical characterization of the major peanut-agglutinin-binding glycoproteins in vertebrate retinae. The Journal of comparative neurology. vol 249. issue 4. 1986-09-29. PMID:3745505. pna binds consistently to domains of the interphotoreceptor matrix associated with cone, but not rod, inner and outer segments, to cone cell body and axonal membranes, to cone synaptic pedicles, and to portions of the inner plexiform layer. 1986-09-29 2023-08-11 human
F Uehara, T Muramatsu, M Ozawa, H Koide, M Sameshima, N Ohb. Purification of antibody against peanut agglutinin-receptors of bovine interphotoreceptor matrix. Japanese journal of ophthalmology. vol 30. issue 1. 1986-08-13. PMID:3088306. immunohistochemical studies revealed that the antibody was bound not only to the surfaces of the cone photoreceptor cells but also to the surfaces of the rods, suggesting that the antibody purified here may have been formed by the major structure of glycoprotein that is common in the interphotoreceptor matrix around the cones and rods. 1986-08-13 2023-08-11 rabbit
D H Anderson, J Neitz, J C Saari, D D Kaska, J Fenwick, G H Jacobs, S K Fishe. Retinoid-binding proteins in cone-dominant retinas. Investigative ophthalmology & visual science. vol 27. issue 7. 1986-08-08. PMID:3721781. this material was particularly prominent near the cone outer segment plasma membranes, and was tentatively identified as the residual interphotoreceptor matrix that remained after exposure to the solvents used during tissue processing. 1986-08-08 2023-08-11 rabbit
L V Johnson, G S Hageman, J C Blank. Interphotoreceptor matrix domains ensheath vertebrate cone photoreceptor cells. Investigative ophthalmology & visual science. vol 27. issue 2. 1986-03-11. PMID:3080382. interphotoreceptor matrix domains ensheath vertebrate cone photoreceptor cells. 1986-03-11 2023-08-11 human
L V Johnson, G S Hageman, J C Blank. Interphotoreceptor matrix domains ensheath vertebrate cone photoreceptor cells. Investigative ophthalmology & visual science. vol 27. issue 2. 1986-03-11. PMID:3080382. these cone extracellular matrix sheaths are chemically and structurally distinct from the remainder of the ipm as revealed by their specific binding of the lectin peanut agglutinin (pna) and their structural stability during physical dissociation of the retina. 1986-03-11 2023-08-11 human
L V Johnson, G S Hageman, J C Blank. Interphotoreceptor matrix domains ensheath vertebrate cone photoreceptor cells. Investigative ophthalmology & visual science. vol 27. issue 2. 1986-03-11. PMID:3080382. biochemical studies suggest that the pna-binding components of the cone matrix sheaths are trypsin-sensitive glycoproteins. 1986-03-11 2023-08-11 human
M J Powell, L P Lehnen, R N Bortnic. Microbody-like organelles as taxonomic markers among Oomycetes. Bio Systems. vol 18. issue 3-4. 1986-02-28. PMID:3910137. these k-bodies lack a granular matrix, but contain a single curved plate from which tubules arise, forming a cone. 1986-02-28 2023-08-11 Not clear
L V Johnson, G S Hageman, J C Blank. Restricted extracellular matrix domains ensheath cone photoreceptors in vertebrate retinae. Progress in clinical and biological research. vol 190. 1985-11-18. PMID:3931096. restricted extracellular matrix domains ensheath cone photoreceptors in vertebrate retinae. 1985-11-18 2023-08-11 Not clear
R D Fernald, S E Wrigh. Growth of the visual system in the African cichlid fish, Haplochromis burtoni. Optics. Vision research. vol 25. issue 2. 1985-08-20. PMID:4013083. this resolution is nearly ten times greater than can be resolved by the cone matrix. 1985-08-20 2023-08-11 Not clear