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Journal of Biological Chemistry, ISSN 0021-9258, 01/2010, 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 | Index Medicus | Mammal | Protein Structure and Folding | Cartilage | Extracellular Matrix | Post-translational Modification | Collagen | Hydroxyproline | Organisms | 3-hydroxyproline | Bone | Protein
Journal Article
Journal of Cell Biology, ISSN 0021-9525, 06/2017, Volume 216, Issue 6, pp. 1761 - 1774
The unfolded protein response (UPR) handles unfolded/misfolded proteins accumulated in the endoplasmic reticulum (ER). However, it is unclear how vertebrates... 
UNFOLDED PROTEIN RESPONSE | NOTOCHORD | MOUSE T-GENE | TRANSCRIPTIONAL INDUCTION | RETICULUM EXIT SITES | ENDOPLASMIC-RETICULUM | MEDAKA FISH | STRESS | TRANSMEMBRANE PROTEIN | CELL BIOLOGY | Basic-Leucine Zipper Transcription Factors - metabolism | Notochord - secretion | Humans | Embryo, Nonmammalian - metabolism | Endoplasmic Reticulum - metabolism | Activating Transcription Factor 6 - genetics | Collagen Type II - metabolism | Oryzias - metabolism | Fish Proteins - genetics | Notochord - metabolism | Transfection | Time Factors | Gene Expression Regulation, Developmental | Collagen Type II - secretion | Transcription, Genetic | Oryzias - genetics | Animals, Genetically Modified | HCT116 Cells | COP-Coated Vesicles - metabolism | Fish Proteins - metabolism | Genotype | Basic-Leucine Zipper Transcription Factors - genetics | Unfolded Protein Response | Basement Membrane - metabolism | Protein Transport | Activating Transcription Factor 6 - metabolism | Phenotype | Animals | COP-Coated Vesicles - secretion | Endoplasmic Reticulum Stress | Vacuoles - metabolism | Oryzias - embryology | Physiological aspects | Embryonic development | Collagen | Exports | Pattern formation | Transducers | Collagen (type II) | Secretion | Chains | Chaperones | Cells | Proteins | Embryonic growth stage | Signal transduction | Vertebrates | Embryogenesis | Protein folding | Fish | Stress response | Endoplasmic reticulum | Notochord | Enlargement | Cargo handling | Index Medicus
Journal Article
Methods in Molecular Biology, ISSN 1064-3745, 2018, Volume 1868, pp. 3 - 7
Due to limitations of using patient-derived samples for systemic kinetic studies in rheumatoid arthritis (RA) research, animal models are helpful for further... 
Freund’s adjuvant | Immunization | Emulsion | Type II collagen | Collagen-induced arthritis | Arthritis, Experimental - pathology | Mice, Inbred DBA | Animals | Emulsions - chemistry | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 10/2007, Volume 282, Issue 43, pp. 31166 - 31173
We have previously reported that COMP ( c artilage o ligomeric m atrix p rotein) is prominent in cartilage but is also present in tendon and binds to collagens... 
FIBRIL FORMATION | IX COLLAGEN | TENDON | CORE PROTEINS | NATIVE COLLAGEN | FIBROMODULIN | ARTICULAR-CARTILAGE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ELECTRON-MICROSCOPY | POLYACRYLAMIDE GELS | OLIGOMERIC MATRIX PROTEIN | Immunohistochemistry | Surface Plasmon Resonance | Temperature | Gold Colloid | Collagen Type I - chemistry | Glycoproteins - metabolism | Hydroxyproline - analysis | Extracellular Matrix Proteins - analysis | Collagen Type II - metabolism | Matrilin Proteins | Time Factors | Cattle | Collagen Type II - isolation & purification | Glycoproteins - isolation & purification | Extracellular Matrix Proteins - isolation & purification | Catalysis | Buffers | Glycoproteins - chemistry | Acids - pharmacology | Extracellular Matrix Proteins - metabolism | Collagen Type II - ultrastructure | Glycoproteins - genetics | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Nephelometry and Turbidimetry | Extracellular Matrix Proteins - chemistry | Collagen Type I - metabolism | Enzyme-Linked Immunosorbent Assay | Electrophoresis, Polyacrylamide Gel | Extracellular Matrix Proteins - genetics | Collagen Type I - isolation & purification | Recombinant Proteins - chemistry | Blotting, Western | Collagen Type I - ultrastructure | Hydrolysis | Particle Size | Collagen - metabolism | Skin - chemistry | Animals | HEPES - chemistry | Collagen Type II - chemistry | Pepsin A - pharmacology | Glycoproteins - analysis | Kinetics | Hydrogen-Ion Concentration | Index Medicus | Rheumatology and Autoimmunity | Clinical Medicine | Other Clinical Medicine | Medical and Health Sciences | Medicin och hälsovetenskap | Reumatologi och inflammation | Annan klinisk medicin | Klinisk medicin
Journal Article
Journal of Immunology, ISSN 0022-1767, 04/2011, Volume 186, Issue 7, pp. 4396 - 4404
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Journal Article
Plant Biotechnology Journal, ISSN 1467-7644, 10/2014, Volume 12, Issue 8, pp. 1143 - 1152
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