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Matrix, ISSN 0934-8832, 1989
Journal
The Journal of biological chemistry, ISSN 1083-351X, 2010, Volume 285, Issue 4, pp. 2580 - 2590
Collagen triple helices are stabilized by 4-hydroxyproline residues. No function is known for the much less common 3-hydroxyproline (3Hyp), although genetic... 
PROLYL 3-HYDROXYLATION | AMINO-ACID-SEQUENCE | ARTICULAR-CARTILAGE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CYANOGEN-BROMIDE PEPTIDES | RECESSIVE OSTEOGENESIS IMPERFECTA | TRIPLE-HELIX | BASEMENT-MEMBRANE COLLAGEN | CARTILAGE COLLAGEN | HIGHER-ORDER STRUCTURES | COVALENT STRUCTURE | Collagen Type V - genetics | Humans | Collagen Type I - chemistry | Collagen Type III - metabolism | Molecular Sequence Data | Collagen - chemistry | Collagen Type XI - chemistry | Collagen Type XI - metabolism | Collagen Type II - metabolism | Young Adult | Tandem Mass Spectrometry | Collagen Type I - genetics | Collagen Type XI - genetics | Cattle | Bone and Bones - metabolism | Adult | Collagen - genetics | Collagen Type V - metabolism | Hydroxyproline - chemistry | Extracellular Matrix Proteins - metabolism | Amino Acid Sequence | Extracellular Matrix Proteins - chemistry | Collagen Type I - metabolism | Collagen Type V - chemistry | Bone and Bones - chemistry | Extracellular Matrix Proteins - genetics | Hydroxyproline - metabolism | Collagen Type III - chemistry | Collagen Type III - genetics | Cartilage - metabolism | Collagen Type II - genetics | Collagen - metabolism | Hydroxyproline - genetics | Animals | Chickens | Cartilage - chemistry | Collagen Type II - chemistry | Protein Processing, Post-Translational | Mammal | Protein Structure and Folding | Cartilage | Extracellular Matrix | Post-translational Modification | Collagen | Hydroxyproline | Organisms | 3-hydroxyproline | Bone | Protein
Journal Article
Advanced materials (Weinheim), ISSN 0935-9648, 2019, Volume 31, Issue 1, pp. 1801651 - n/a
Journal Article
Clinical Oral Implants Research, ISSN 0905-7161, 10/2018, Volume 29, Issue S17, pp. 315 - 315
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 06/2012, Volume 287, Issue 27, pp. 22549 - 22559
The tensile and scaffolding properties of skin rely on the complex extracellular matrix (ECM) that surrounds cells, vasculature, nerves, and adnexus structures... 
MULTIPLE EPIPHYSEAL DYSPLASIA | IX COLLAGEN | COMP | CAUSE PSEUDOACHONDROPLASIA | DIFFERENTIAL EXPRESSION | TENASCIN-X | ANCHORING FIBRILS | BIOCHEMISTRY & MOLECULAR BIOLOGY | VII COLLAGEN | ENDOPLASMIC-RETICULUM | SYSTEMIC-SCLEROSIS | Surface Plasmon Resonance | Humans | Glycoproteins - metabolism | Child, Preschool | Extracellular Matrix - metabolism | Collagen - chemistry | Infant | Microscopy, Immunoelectron | Matrilin Proteins | Collagen Type I - genetics | HEK293 Cells | Collagen - genetics | Glycoproteins - chemistry | Extracellular Matrix Proteins - metabolism | Fibroblasts - metabolism | Glycoproteins - genetics | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Extracellular Matrix Proteins - chemistry | Collagen Type I - metabolism | Dermis - metabolism | Cartilage Oligomeric Matrix Protein | Extracellular Matrix Proteins - genetics | Recombinant Proteins - genetics | Dermis - ultrastructure | Basement Membrane - metabolism | Collagen - metabolism | Collagen Type XII - chemistry | Animals | Keratinocytes - metabolism | Collagen Type XII - genetics | Collagen Type XII - metabolism | Mice | Collagen I Fibril | FACIT Collagens | Surface Plasmon Resonance (SPR) | Extracellular Matrix | Collagen | Anchoring Plaques | Glycobiology and Extracellular Matrices | Skin | Fibroblast | Rheumatology and Autoimmunity | Clinical Medicine | Medical and Health Sciences | Klinisk medicin | Medicin och hälsovetenskap | Reumatologi och inflammation
Journal Article
Biophysical Journal, ISSN 0006-3495, 02/2017, Volume 112, Issue 3, pp. 238a - 238a
Journal Article
Cold Spring Harbor perspectives in biology, ISSN 1943-0264, 2010, Volume 3, Issue 1, pp. a004978 - a004978
Collagens are the most abundant proteins in mammals. The collagen family comprises 28 members that contain at least one triple-helical domain. Collagens are... 
CROSS-LINK | CRYSTAL-STRUCTURE | ENDOTHELIAL-CELLS | DOMAIN RECEPTOR 2 |