Results 261 to 270 of about 351,215 (306)
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Type I and Type III Collagens in Cutaneous Mucinosis
The American Journal of Dermatopathology, 1998Cutaneous mucinoses are a heterogeneous group of diseases characterized by the focal or diffuse dermal deposition of glycosaminoglycans. The histopathologic examination of many cutaneous mucinoses reveals that the collagen fibers are fragmented. We wanted to characterize the type I (COL1) and type III (COL3) collagen distribution in skin biopsy ...
M F, Alves +3 more
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Dermal collagen fibrils are hybrids of type I and type III collagen molecules
Journal of Structural Biology, 1990It has been suggested that dermal collagen fibrils with 67-nm periodicity consist of hybrids of type I and type III collagens. This is based on the assumption that all these banded fibrils are coated with type III collagen regardless of their diameter. However, conclusive evidence for this form of hybridization is lacking.
R, Fleischmajer +4 more
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The presence of type III collagen in the developing tooth
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1978Type I and type III collagens have been isolated from dental papilla and dental pulp of bovine tissues by enzymic digestion with pepsin and differential salt precipitation. Type III collagen was further purified by molecular sieve and ion-exchange chromatography.
C A, Shuttleworth +2 more
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Crosslinking in type III collagen of fetal tissue
Biochemical and Biophysical Research Communications, 1978Abstract Native bovine amnion tissue was reduced with NaB 3 H 4 and type III collagen was isolated by pepsin digestion. Examination of the crosslink content of type III collagen following acid hydrolysis revealed the presence of dihydroxy- and hydroxylysinonorleucine in a ratio of 9 to 1.
D J, Cannon, P F, Davison
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Demonstration of type III collagen in the dentin of mice
Matrix, 1992It has been reported that, although type III collagen is present in human dentin where there is dentinogenesis imperfecta and in reparative dentin, it is absent in normal dentin. In a preliminary study, however, we observed evidence showing that small amounts of fibers showing positive labeling for type III collagen are present in the molars of normal ...
K, Nagata +5 more
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Studies on the sulfhydryl groups in type III collagen
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1976The Type III collagen molecule, [alpha](III)]3, is comprised of three alphal(III) chains each of which contains two cysteinyl residues. Free sulfhydryl groups, however, could not be detected in the denatured, trimeric gamma-component of Type III collagen as judged by the failure to form derivatives with the alkylating reagents iodo-[14C]acetic acid and
M, Schneir, E J, Miller
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Covalent binding of acetaldehyde to type III collagen
Biochemical and Biophysical Research Communications, 1989Incubation of neutral salt soluble type III pN-collagen with [14C]acetaldehyde in vitro resulted in the formation of spontaneously stable acetaldehyde-protein adducts. This reaction occurred primarily at lysine residues and it was not affected by 0.2-2 mM concentrations of ascorbate but addition of sodiumcyanoborohydride increased the stable adducts by
A, Jukkola, O, Niemelä
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Conformational selection and collagenolysis in Type III collagen
Proteins: Structure, Function, and Bioinformatics, 2009AbstractMatrix metalloproteases (MMPs) cleave native collagen at a single site despite the fact that collagen contains more than one scissile bond that can, in principle, be cleaved. For peptide bond hydrolysis to occur at one specific site, MMPs must (1) localize to a region near the unique scissile bond, (2) bind residues at the catalytic site that ...
Ramon, Salsas-Escat, Collin M, Stultz
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Role of type III collagen in bladder filling
Neurourology and Urodynamics, 1998The function of the urinary bladder is to store urine at low pressure and expel it periodically. To accomplish this, it must have the appropriate structural properties to accommodate slow but continuous volume changes. While much is presently known about the functional measurements of compliance, relatively little is known about the structural basis of
S L, Chang +3 more
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Bovine dental pulp collagens: Characterization of types III and V collagen
Archives of Oral Biology, 1990Pulp was essentially solubilized by partial pepsin digestion. The various genetic types of collagens were isolated by differential salt precipitation and extraction. Types I, III and V collagen represented 56, 41 and 2% of the total collagen, respectively. The type V collagen comprised two different molecular species consisting of [alpha 1(V)]2 alpha 2(
M, Tsuzaki, M, Yamauchi, G L, Mechanic
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