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animals (102) 102
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heat-shock proteins - metabolism (45) 45
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1. Full Text Biology of Hsp47 (Serpin H1), a collagen-specific molecular chaperone
by Ito, Shinya and Nagata, Kazuhiro
Seminars in Cell and Developmental Biology, ISSN 1084-9521, 02/2017, Volume 62, pp. 142 - 151
Hsp47, a collagen-specific molecular chaperone that localizes in the endoplasmic reticulum (ER), is indispensable for molecular maturation of collagen. Hsp47,... 
Osteogenesis imperfecta | Serpin | Collagen | Molecular chaperone | Heat-shock protein | Fibrosis | EMBRYO FIBROBLASTS | STRESS-PROTEIN HSP47 | TRIPLE-HELIX | I COLLAGEN | DEVELOPMENTAL BIOLOGY | QUALITY-CONTROL | HEAT-SHOCK-PROTEIN | CELL BIOLOGY | BINDING GLYCOPROTEIN | MISFOLDED PROCOLLAGEN | ENDOPLASMIC-RETICULUM | Collagen - metabolism | Phenotype | Animals | HSP47 Heat-Shock Proteins - chemistry | Disease | Models, Biological | Humans | Protein Binding | HSP47 Heat-Shock Proteins - metabolism | Thrombin | Glycine | Liver
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2. Full Text Hsp47 as a Collagen-Specific Molecular Chaperone
by Ishida, Yoshihito and Nagata, Kazuhiro
2011, Methods in Enzymology, ISBN 9780123864710, Volume 499, 16
Heat shock protein (HSP) 47 is a 47 kDa collagen-binding glycoprotein localized in the endoplasmic reticulum (ER). It belongs to the serpin family and contains... 
Serpin H1 | Collagen-related disorder | Hsp47 | Collagen | Autophagy | Endoplasmic reticulum | Molecular chaperone | EMBRYO FIBROBLASTS | MISFOLDED PROCOLLAGEN | RETICULUM-ASSOCIATED DEGRADATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | CONSTITUTIVE AUTOPHAGY | BIOCHEMICAL RESEARCH METHODS | TRIPLE-HELIX | BINDING STRESS-PROTEIN | ENDOPLASMIC-RETICULUM | I COLLAGEN | DIABETIC-NEPHROPATHY | HEAT-SHOCK-PROTEIN | Molecular Chaperones - metabolism | Humans | Molecular Chaperones - genetics | Endoplasmic Reticulum - metabolism | HSP47 Heat-Shock Proteins - genetics | Protein Folding | Mice, Knockout | Collagen - metabolism | Animals | Models, Biological | Protein Binding | HSP47 Heat-Shock Proteins - metabolism | Mice
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3. Full Text Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition
by Christine Widmer and Jan M. Gebauer and Elena Brunstein and Sabrina Rosenbaum and Frank Zaucke and Cord Drögemüller and Tosso Leeb and Ulrich Baumann
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2012, Volume 109, Issue 33, pp. 13243 - 13247
Collagen is the most abundant protein in animals and is a major component of the extracellular matrix in tissues such as skin and bone. A distinctive... 
Proteins | Molecules | Salts | Molecular chaperones | Collagens | Atoms | Antibodies | Biochemistry | Binding sites | Crystal structure | Protein stability | Protein folding | Protein-protein interactions | Serpins | MULTIDISCIPLINARY SCIENCES | IV COLLAGEN | TRIPLE-HELIX | BINDING STRESS-PROTEIN | PHENIX | protein stability | protein-protein interactions | REFINEMENT | PEPTIDES | HSP47 | protein folding | DIFFERENTIATION | Amino Acid Sequence | Collagen Type I - metabolism | HSP47 Heat-Shock Proteins - chemistry | Peptides - chemistry | Protein Structure, Secondary | Collagen Type I - chemistry | Models, Molecular | Molecular Sequence Data | Rats | Substrate Specificity | Mutant Proteins - metabolism | Structure-Activity Relationship | Mutation, Missense - genetics | Animals | Peptides - metabolism | Dogs | Hydrophobic and Hydrophilic Interactions | Protein Binding | HSP47 Heat-Shock Proteins - metabolism | Mice | Binding Sites | Collagen | Physiological aspects | Molecular dynamics | Research | Health aspects | protein–protein interactions | Biological Sciences
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4. Full Text Hsp47 mediates Cx43-dependent skeletal growth and patterning in the regenerating fin
by Bhadra, Joyita and Iovine, M. Kathryn
Mechanisms of Development, ISSN 0925-4773, 11/2015, Volume 138, pp. 364 - 374
Skeletal morphogenesis describes how bones achieve their correct shape and size and appropriately position joints. We use the regenerating caudal fin of... 
Cell proliferation | Joint formation | short fin | Zebrafish | Gap junction | Short fin | OCULODENTODIGITAL DYSPLASIA | COLLAGEN | STRESS-PROTEIN HSP47 | PROLIFERATION | DEVELOPMENTAL BIOLOGY | CONNEXIN43 GJA1 | MOLECULAR CHAPERONE HSP47 | MORPHOGENESIS | GAP-JUNCTIONS | ZEBRAFISH CAUDAL FIN | PROCOLLAGEN | Animal Fins - growth & development | Cell Proliferation | Bone Development - physiology | RNA, Messenger - metabolism | Gene Knockdown Techniques | Connexin 43 - physiology | In Situ Hybridization | Regeneration - genetics | Connexin 43 - genetics | Signal Transduction | Animals, Genetically Modified | RNA, Messenger - genetics | Zebrafish Proteins - antagonists & inhibitors | HSP47 Heat-Shock Proteins - antagonists & inhibitors | Regeneration - physiology | HSP47 Heat-Shock Proteins - genetics | Zebrafish - growth & development | Zebrafish - genetics | Zebrafish Proteins - physiology | Body Patterning - physiology | HSP47 Heat-Shock Proteins - physiology | Animal Fins - physiology | Animals | Models, Biological | Zebrafish - physiology | Bone Development - genetics | Mutation | Zebrafish Proteins - genetics | Body Patterning - genetics | Growth | Collagen
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5. Full Text Specific recognition of the collagen triple helix by chaperone HSP47: Minimal structural requirement and spatial molecular orientation
by Koide, Takaki and Asada, Shinichi and Takahara, Yoshifumi and Nishikawa, Yoshimi and Nagata, Kazuhiro and Kitagawa, Kouki
Journal of Biological Chemistry, ISSN 0021-9258, 02/2006, Volume 281, Issue 6, pp. 3432 - 3438
The unique folding of procollagens in the endoplasmic reticulum is achieved with the assistance of procollagen-specific molecular chaperones. Heat-shock... 
STRESS-PROTEIN HSP47 | SITES | PEPTIDES | PROCOLLAGEN | BIOCHEMISTRY & MOLECULAR BIOLOGY | Surface Plasmon Resonance | HSP47 Heat-Shock Proteins - chemistry | Molecular Chaperones - metabolism | Models, Chemical | Cross-Linking Reagents - pharmacology | Humans | Endoplasmic Reticulum - metabolism | Molecular Sequence Data | Collagen - chemistry | Ultraviolet Rays | Escherichia coli - metabolism | Circular Dichroism | Binding, Competitive | Amino Acid Sequence | Peptides - chemistry | Electrophoresis, Polyacrylamide Gel | Models, Molecular | Recombinant Proteins - chemistry | Blotting, Western | Chromatography | Protein Folding | Arginine - chemistry | Sequence Homology, Amino Acid | Animals | Protein Binding | Protein Conformation | Mice | Spectrophotometry
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6. Full Text Photoactivatable Hsp47: A Tool to Regulate Collagen Secretion and Assembly
by Khan, Essak S and Sankaran, Shrikrishnan and Paez, Julieta I and Muth, Christina and Han, Mitchell K. L and del Campo, Aránzazu
Advanced Science, ISSN 2198-3844, 05/2019, Volume 6, Issue 9, pp. 1801982 - n/a
Collagen is the most abundant structural protein in mammals and is crucial for the mechanical integrity of tissues. Hsp47, an endoplasmic reticulum resident... 
collagen deposition | noncanonical amino acid incorporation | photoactivation | Hsp47 | KDEL receptor‐mediated endocytosis | KDEL receptor-mediated endocytosis | CELLS | MATERIALS SCIENCE, MULTIDISCIPLINARY | INVOLVEMENT | STRESS-PROTEIN HSP47 | TRIPLE-HELIX | SENSITIVITY | NANOSCIENCE & NANOTECHNOLOGY | MECHANISMS | CHAPERONE HSP47 | CHEMISTRY, MULTIDISCIPLINARY | I PROCOLLAGEN | ENDOPLASMIC-RETICULUM | BINDING | Proteins | Tissue engineering | Collagen | Light | Fibroblasts | Amino acids | Biosynthesis | Genetic engineering | Mutation | Binding sites
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7. Full Text Detection of substrate binding of a collagen-specific molecular chaperone HSP47 in solution using fluorescence correlation spectroscopy
by Kitamura, Akira and Ishida, Yoshihito and Kubota, Hiroshi and Pack, Chan-Gi and Homma, Takayuki and Ito, Shinya and Araki, Kazutaka and Kinjo, Masataka and Nagata, Kazuhiro
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 02/2018, Volume 497, Issue 1, pp. 279 - 284
Heat shock protein 47 kDa (HSP47), an ER-resident and collagen-specific molecular chaperone, recognizes collagenous hydrophobic amino acid sequences... 
HSP47 | Collagen | Molecular chaperone | Fluorescence correlation spectroscopy | FIBROSIS | RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | STRESS-PROTEIN HSP47 | TRIPLE-HELIX | CROSS-CORRELATION SPECTROSCOPY | I COLLAGEN | BIOPHYSICS | ENDOPLASMIC-RETICULUM | MUTATIONS | LIVING CELLS
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8. Full Text The molecular chaperone Hsp47 is essential for cartilage and endochondral bone formation
by Masago, Yusaku and Hosoya, Akihiro and Kawasaki, Kunito and Kawano, Shogo and Nasu, Akira and Toguchida, Junya and Fujita, Katsumasa and Nakamura, Hiroaki and Kondoh, Gen and Nagata, Kazuhiro
Journal of Cell Science, ISSN 0021-9533, 03/2012, Volume 125, Issue 5, pp. 1118 - 1128
Heat shock protein 47 kDa (Hsp47) is considered as a molecular chaperone essential for the correct folding of type I and type IV procollagen in the ER.... 
Cartilage | Hsp47 | Endochondral bone | Collagen | Intervertebral disc | STRESS-PROTEIN HSP47 | TRIPLE-HELIX | TRANSMEMBRANE DOMAIN | CELL BIOLOGY | MULTIPLE EPIPHYSEAL DYSPLASIA | COLLAGEN-BINDING PROTEIN | CARBOXYL-TERMINAL PROPEPTIDE | II COLLAGEN | COL2A1 GENE | ENDOPLASMIC-RETICULUM | TRANSGENIC MICE | Cartilage - embryology | Osteogenesis - physiology | Mice, Inbred C57BL | Cells, Cultured | Cartilage - metabolism | HSP47 Heat-Shock Proteins - genetics | Collagen Type II - genetics | Protein Folding | Mice, Knockout | Chondrogenesis - physiology | Collagen Type I - biosynthesis | Animals | Collagen Type I - genetics | Bone and Bones - metabolism | Collagen Type XI - biosynthesis | HSP47 Heat-Shock Proteins - metabolism | Mice | Bone and Bones - embryology | Chondrocytes - metabolism | Collagen Type II - biosynthesis
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9. Full Text Mutants of collagen-specific molecular chaperone Hsp47 causing osteogenesis imperfecta are structurally unstable with weak binding affinity to collagen
by Ito, Shinya and Nagata, Kazuhiro
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 01/2016, Volume 469, Issue 3, pp. 437 - 442
Osteogenesis imperfecta (OI) is a genetic disorder characterized by fragile bones. Most OI cases are caused by defects in type I collagen structure or... 
Osteogenesis imperfecta | ER stress | Chemical chaperone | Molecular chaperone Hsp47 | Collagen | FIBROSIS | CELLS | A-COUPLED LIPOSOMES | BIOCHEMISTRY & MOLECULAR BIOLOGY | STRESS-PROTEIN HSP47 | MODEL | BIOPHYSICS | GENES | ENDOPLASMIC-RETICULUM | SIRNA | Animals | Collagen Type I - genetics | Collagen Type I - metabolism | Humans | Osteogenesis Imperfecta - physiopathology | Protein Binding | HSP47 Heat-Shock Proteins - metabolism | Mice | Mutation - genetics | Binding Sites | HSP47 Heat-Shock Proteins - genetics | Ubiquitin
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10. Full Text Hsp47: a molecular chaperone that interacts with and stabilizes correctly‐folded procollagen
by Tasab, Mohammed and Batten, Margaret R and Bulleid, Neil J
The EMBO Journal, ISSN 0261-4189, 05/2000, Volume 19, Issue 10, pp. 2204 - 2211
Hsp47 is a heat‐shock protein that interacts transiently with procollagen during its folding, assembly and transport from the endoplasmic reticulum (ER) of... 
procollagen | molecular chaperone | protein folding | Hsp47 | Procollagen | Protein folding | Molecular chaperone | CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | COLLAGEN TRIPLE-HELIX | III PROCOLLAGEN | STRESS PROTEIN HSP47 | QUALITY-CONTROL | CELL BIOLOGY | CARBOXYL-TERMINAL PROPEPTIDE | I PROCOLLAGEN | ENDOPLASMIC-RETICULUM | OSTEOGENESIS IMPERFECTA | PROLYL 4-HYDROXYLASE | Recombinant Proteins - metabolism | Rabbits | Animals | Molecular Chaperones - metabolism | Heat-Shock Proteins - metabolism | Procollagen - chemistry | Protein Binding | Recombinant Proteins - chemistry | Procollagen - metabolism | Molecular Chaperones - chemistry | Protein Folding | Heat-Shock Proteins - chemistry
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11. Full Text Treatment of pulmonary fibrosis with siRNA against a collagen-specific chaperone HSP47 in vitamin A-coupled liposomes
by Otsuka, Mitsuo and Shiratori, Masanori and Chiba, Hirofumi and Kuronuma, Koji and Sato, Yasushi and Niitsu, Yoshiro and Takahashi, Hiroki
Experimental Lung Research, ISSN 0190-2148, 08/2017, Volume 43, Issue 6-7, pp. 271 - 282
Background: Pulmonary fibrosis is a life-threatening pathological state of progressive interstitial lung diseases, such as idiopathic pulmonary fibrosis.... 
siRNA | Bleomycin | HSP47 | pulmonary fibrosis | LUNG | INDUCED PNEUMONOPATHY | STRESS-PROTEIN HSP47 | INTERSTITIAL PNEUMONIA | HEPATIC STELLATE CELLS | RESPIRATORY SYSTEM | MOLECULAR CHAPERONE | ENDOPLASMIC-RETICULUM | ANTISENSE OLIGONUCLEOTIDES | EXPRESSION | BINDING HEAT-SHOCK-PROTEIN-47 | Vitamin A - pharmacology | Molecular Chaperones - metabolism | Cytokines - metabolism | Hydroxyproline - metabolism | RNA, Small Interfering - pharmacology | Rats | Male | Myofibroblasts - drug effects | Rats, Sprague-Dawley | Myofibroblasts - metabolism | Collagen - metabolism | Inflammation - metabolism | Animals | Inflammation - drug therapy | Lung - drug effects | Bleomycin - pharmacology | HSP47 Heat-Shock Proteins - metabolism | Lung - metabolism | Pulmonary Fibrosis - metabolism | Bronchoalveolar Lavage Fluid - chemistry | Pulmonary Fibrosis - drug therapy | Liposomes - pharmacology
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12. Full Text Embryonic Lethality of Molecular Chaperone Hsp47 Knockout Mice Is Associated with Defects in Collagen Biosynthesis
by Naoko Nagai and Masanori Hosokawa and Shigeyoshi Itohara and Eijiro Adachi and Takatoshi Matsushita and Nobuko Hosokawa and Kazuhiro Nagata
The Journal of Cell Biology, ISSN 0021-9525, 9/2000, Volume 150, Issue 6, pp. 1499 - 1505
Triple helix formation of procollagen after the assembly of three α-chains at the C-propeptide is a prerequisite for refined structures such as fibers and... 
Molecular chaperones | Neurons | Collagens | Cell lines | Reports | Mice | Solar fibrils | Embryos | Endothelial cells | Cells | Basement membrane | Extracellular matrix | Gene targeting | Collagen fibril | Type I collagen | basement membrane | collagen fibril | IV COLLAGEN | CALNEXIN | gene targeting | STRESS PROTEIN HSP47 | type I collagen | LAMINA DENSA | MOUSE EMBRYO | CELL BIOLOGY | GENE | ALPHA-1(I) | ENDOPLASMIC-RETICULUM | PROCOLLAGEN | EXPRESSION | extracellular matrix | Physiological aspects | Genetic aspects | Collagen diseases | Collagen
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13. Full Text The collagen-specific molecular chaperone HSP47: is there a role in fibrosis?
by Taguchi, Takashi and Razzaque, M. Shawkat
Trends in Molecular Medicine, ISSN 1471-4914, 2006, Volume 13, Issue 2, pp. 45 - 53
Heat shock protein 47 (HSP47) is a collagen-specific molecular chaperone that is required for molecular maturation of various types of collagens. Recent... 
Pathology | MEDICINE, RESEARCH & EXPERIMENTAL | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRIPLE-HELIX | BINDING STRESS-PROTEIN | DISULFIDE-ISOMERASE SUBUNIT | MESSENGER-RNA LEVELS | HEAT-SHOCK-PROTEIN | CELL BIOLOGY | INDUCED PULMONARY-FIBROSIS | TRANSFORMING GROWTH-FACTOR-BETA-1 | ENDOPLASMIC-RETICULUM | PROLYL 4-HYDROXYLASES | ANTISENSE OLIGONUCLEOTIDES | Collagen - metabolism | Fibrosis - therapy | Animals | Models, Biological | Fibrosis - etiology | Humans | HSP47 Heat-Shock Proteins - metabolism | Protein Processing, Post-Translational | Fibrosis - metabolism
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14. Pirfenidone attenuates expression of HSP47 in murine bleomycin-induced pulmonary fibrosis
by Kakugawa, T and Mukae, H and Hayashi, T and Ishii, H and Abe, K and Fujii, T and Oku, H and Miyazaki, M and Kadota, J and Kohno, S
European Respiratory Journal, ISSN 0903-1936, 07/2004, Volume 24, Issue 1, pp. 57 - 65
Heat shock protein (HSP) 47, a collagen-specific molecular chaperone, is involved in the processing and/or secretion of procollagen. The present study was... 
α-smooth muscle actin | Heat shock protein 47 | Pulmonary fibrosis | Pirfenidone | Myofibroblast | alpha-smooth muscle actin | SMOOTH MUSCLE ACTIN | LUNG FIBROSIS | myofibroblast | STRESS-PROTEIN HSP47 | HEAT-SHOCK-PROTEIN | COLLAGEN-BINDING HEAT-SHOCK-PROTEIN-47 | heat shock protein 47 | GRANULATION-TISSUE | pirfenidone | RESPIRATORY SYSTEM | pulmonary fibrosis | MYOFIBROBLASTS | GROWTH-FACTOR | ANTISENSE OLIGONUCLEOTIDES | PROCOLLAGEN | Immunohistochemistry | Injections, Intravenous | Hydroxyproline - metabolism | Probability | Hydroxyproline - analysis | Male | Reference Values | Pulmonary Fibrosis - pathology | Random Allocation | Mice, Inbred Strains | HSP70 Heat-Shock Proteins - metabolism | Animals | Bleomycin | Analysis of Variance | HSP70 Heat-Shock Proteins - drug effects | Sensitivity and Specificity | Mice | Biopsy, Needle | Pulmonary Fibrosis - drug therapy | Pyridones - pharmacology | Disease Models, Animal
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15. Full Text Localization of HSP47 mRNA in murine bleomycin-induced pulmonary fibrosis
by Kakugawa, Tomoyuki and Mukae, Hiroshi and Hishikawa, Yoshitaka and Ishii, Hiroshi and Sakamoto, Noriho and Ishimatsu, Yuji and Fujii, Takeshi and Koji, Takehiko and Kohno, Shigeru
Virchows Archiv, ISSN 0945-6317, 3/2010, Volume 456, Issue 3, pp. 309 - 315
Heat shock protein 47 (HSP47) is a collagen-specific molecular chaperone that has been shown to play a major role in the processing and/or secretion of... 
Pathology | Pulmonary fibrosis | Heat shock protein 47 | Medicine & Public Health | In situ hybridization | COLLAGEN | INCREASED EXPRESSION | IN-SITU HYBRIDIZATION | BINDING STRESS-PROTEIN | PATHOLOGY | HEAT-SHOCK-PROTEIN | GROWTH-FACTOR | ANTISENSE OLIGONUCLEOTIDES | PROCOLLAGEN | HEAT-SHOCK-PROTEIN-47 | TRANSDIFFERENTIATION | Lung - pathology | Animals | Bleomycin | In Situ Hybridization | Pulmonary Fibrosis - physiopathology | Pulmonary Fibrosis - chemically induced | Male | Mice | RNA, Messenger - metabolism | HSP47 Heat-Shock Proteins - genetics | Mice, Inbred ICR | Fibroblasts - metabolism | Messenger RNA | Environmental health | Heat shock proteins | Respiratory tract diseases | Universities and colleges | Macrophages | Secretion | Lung | Lung diseases | Parenchyma | procollagen | mRNA | Chaperones | Collagen | Fibrosis | pneumocytes
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16. Full Text HSP47 as a collagen-specific molecular chaperone: function and expression in normal mouse development
by Nagata, Kazuhiro
Seminars in Cell and Developmental Biology, ISSN 1084-9521, 2003, Volume 14, Issue 5, pp. 275 - 282
A large family of molecular chaperones can be divided into two major groups: general chaperone and substrate-specific chaperone. HSP47 is a collagen-specific... 
HSP47 | Collagen | Molecular chaperone | Mouse development | EMBRYO FIBROBLASTS | collagen | BINDING STRESS-PROTEIN | I COLLAGEN | PRO-ALPHA-1(I) CHAIN | DEVELOPMENTAL BIOLOGY | HEAT-SHOCK-PROTEIN | CELL BIOLOGY | molecular chaperone | CARBOXYL-TERMINAL PROPEPTIDE | INTRACELLULAR INTERACTION | ENDOPLASMIC-RETICULUM | OSTEOGENESIS IMPERFECTA | mouse development | UP-REGULATION | Molecular Chaperones - metabolism | Heat-Shock Proteins - metabolism | HSP47 Heat-Shock Proteins | Molecular Chaperones - genetics | Endoplasmic Reticulum - metabolism | Procollagen - metabolism | Basement Membrane - metabolism | Embryonic and Fetal Development | Protein Folding | Collagen - metabolism | Heat-Shock Proteins - genetics | Animals | Mice | Microfibrils - metabolism
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