arginine and Cutis Elastica

arginine has been researched along with Cutis Elastica in 8 studies

Research

Studies (8)

TimeframeStudies, this research(%)All Research%
pre-19901 (12.50)18.7374
1990's3 (37.50)18.2507
2000's4 (50.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Faiyaz-Ul-Haque, M; Götte, M; Hansen, U; Kiesel, L; Seidler, DG; Teebi, AS; Yip, GW; Zaidi, SH1
Coucke, P; De Backer, J; De Paepe, A; Hermanns-Lê, T; Lapière, CM; Malfait, F; Sakalihasan, N; Symoens, S1
Hermanns-Lê, T; Piérard, GE1
Ferguson, C; Lloyd, J; Narcisi, P; Pope, FM; Richards, A1
Cole, WG1
Bateman, JF; Chan, D; Chiodo, AA; Haan, E; Weng, YM1
De Paepe, A; Freund, M; Hermanns-Le, T; Lagae, L; Nuytinck, L; Pierard, GE1
Kuivaniemi, H; Prockop, DJ; Shikata, H; Tromp, G1

Other Studies

8 other study(ies) available for arginine and Cutis Elastica

ArticleYear
Defective glycosylation of decorin and biglycan, altered collagen structure, and abnormal phenotype of the skin fibroblasts of an Ehlers-Danlos syndrome patient carrying the novel Arg270Cys substitution in galactosyltransferase I (beta4GalT-7).
    Journal of molecular medicine (Berlin, Germany), 2006, Volume: 84, Issue:7

    Topics: Arginine; Biglycan; Cell Proliferation; Cells, Cultured; Collagen; Decorin; Ehlers-Danlos Syndrome; Extracellular Matrix Proteins; Fibroblasts; Galactosyltransferases; Glycosylation; Humans; Microscopy, Electron, Transmission; Phenotype; Proteoglycans; Skin; Temperature

2006
Three arginine to cysteine substitutions in the pro-alpha (I)-collagen chain cause Ehlers-Danlos syndrome with a propensity to arterial rupture in early adulthood.
    Human mutation, 2007, Volume: 28, Issue:4

    Topics: Adolescent; Adult; Amino Acid Substitution; Arginine; Base Sequence; Bone Diseases, Metabolic; Collagen; Collagen Type I; Collagen Type I, alpha 1 Chain; Collagen Type III; Cysteine; Ehlers-Danlos Syndrome; Female; Femoral Artery; Humans; Iliac Artery; Male; Molecular Sequence Data; Mutation, Missense; Protein Structure, Secondary; RNA, Messenger; Rupture, Spontaneous

2007
Multifaceted dermal ultrastructural clues for Ehlers-Danlos syndrome with arterial rupture and type I collagen R-to-C substitution.
    The American Journal of dermatopathology, 2007, Volume: 29, Issue:5

    Topics: Adult; Aneurysm, Ruptured; Aortic Dissection; Arginine; Biopsy; Collagen Type I; Cysteine; Ehlers-Danlos Syndrome; Humans; Skin

2007
The substitution of glycine 661 by arginine in type III collagen produces mutant molecules with different thermal stabilities and causes Ehlers-Danlos syndrome type IV.
    Journal of medical genetics, 1993, Volume: 30, Issue:8

    Topics: Arginine; Base Sequence; Collagen; Ehlers-Danlos Syndrome; Female; Glycine; Hot Temperature; Humans; Molecular Sequence Data; Point Mutation

1993
The Nicholas Andry Award-1996. The molecular pathology of osteogenesis imperfecta.
    Clinical orthopaedics and related research, 1997, Issue:343

    Topics: 3T3 Cells; Animals; Arginine; Awards and Prizes; Bone and Bones; Cells, Cultured; Child; Collagen; Cysteine; Ehlers-Danlos Syndrome; Extracellular Matrix; Extracellular Matrix Proteins; Fibroblasts; Genotype; Glycine; Humans; Infant; Mice; Mice, Transgenic; Molecular Biology; Mutation; Osteogenesis Imperfecta; Phenotype; Point Mutation; Procollagen; Radiography; RNA; Skin

1997
A type III collagen Gly559 to Arg helix mutation in Ehler's-Danlos syndrome type IV.
    Human mutation, 1998, Volume: Suppl 1

    Topics: Amino Acid Substitution; Arginine; Collagen; DNA Mutational Analysis; DNA, Complementary; Ehlers-Danlos Syndrome; Glycine; Humans; Male; Mutation; Point Mutation; RNA, Messenger

1998
Classical Ehlers-Danlos syndrome caused by a mutation in type I collagen.
    American journal of human genetics, 2000, Volume: 66, Issue:4

    Topics: Amino Acid Motifs; Amino Acid Sequence; Amino Acid Substitution; Arginine; Base Sequence; Child; Child, Preschool; Collagen; Cysteine; Dimerization; Disulfides; DNA Mutational Analysis; Ehlers-Danlos Syndrome; Exons; Female; Fibroblasts; Genetic Heterogeneity; Humans; Male; Mutation; Polymorphism, Single-Stranded Conformational

2000
A single base mutation that substitutes serine for glycine 790 of the alpha 1 (III) chain of type III procollagen exposes an arginine and causes Ehlers-Danlos syndrome IV.
    The Journal of biological chemistry, 1989, Jan-25, Volume: 264, Issue:3

    Topics: Arginine; Base Sequence; Codon; DNA; Ehlers-Danlos Syndrome; Glycine; Humans; Molecular Sequence Data; Procollagen; RNA, Messenger; Serine

1989