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Journal Article
Annals of the Rheumatic Diseases, ISSN 0003-4967, 07/2015, Volume 74, Issue 7, pp. 1408 - 1416
ObjectivesWe have previously described the antifibrotic role of the soluble guanylate cyclase (sGC). The mode of action, however, remained elusive. In the... 
GROWTH-FACTOR-BETA | TRANS-DIFFERENTIATION | FIBROTIC DISORDERS | DISEASE | KINASE | EXPERIMENTAL DERMAL FIBROSIS | RHEUMATOLOGY | SYSTEMIC-SCLEROSIS | HYPERTENSION | INDUCED FIBROBLAST ACTIVATION | MAP Kinase Signaling System - physiology | Receptors, Cytoplasmic and Nuclear - deficiency | Skin - metabolism | Humans | Scleroderma, Systemic - pathology | Fibrosis - metabolism | Case-Control Studies | Scleroderma, Systemic - physiopathology | Transforming Growth Factor beta - antagonists & inhibitors | Fibrosis - prevention & control | Skin - pathology | Disease Models, Animal | Fibroblasts - metabolism | Pyrazoles - pharmacology | Scleroderma, Systemic - metabolism | Cells, Cultured | Guanylate Cyclase - metabolism | Soluble Guanylyl Cyclase | Receptors, Cytoplasmic and Nuclear - agonists | Fibroblasts - pathology | Mice, Knockout | Collagen - metabolism | Guanylate Cyclase - deficiency | Animals | MAP Kinase Signaling System - drug effects | Cyclic GMP - metabolism | Receptors, Transforming Growth Factor beta - drug effects | Receptors, Transforming Growth Factor beta - metabolism | Signal Transduction - drug effects | Signal Transduction - physiology | Mice | Pyridines - pharmacology | In Vitro Techniques | Smad Proteins - metabolism | Transforming Growth Factor beta - metabolism | Receptors, Cytoplasmic and Nuclear - metabolism | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 2013, Volume 504, Issue 7480, pp. 432 - 436
Journal Article
PLoS ONE, ISSN 1932-6203, 07/2013, Volume 8, Issue 7, pp. e70223 - e70223
Guanylyl cyclases (GCs) regulate many physiological processes by catalyzing the synthesis of the second messenger cGMP. The GC family consists of seven... 
SITE | SUBSTRATE-SPECIFICITY | ACTIVATION | TOXIN | MULTIDISCIPLINARY SCIENCES | NATRIURETIC-PEPTIDE RECEPTOR | CATALYTIC DOMAIN | INHIBITORS | BORDETELLA-PERTUSSIS | BINDING | RAT LUNG | Cell Line | Receptors, Atrial Natriuretic Factor - metabolism | Humans | Rats | Substrate Specificity | Guanylate Cyclase - metabolism | Soluble Guanylyl Cyclase | Cell Membrane - enzymology | Bacterial Toxins - metabolism | Animals | Cyclic GMP | HEK293 Cells | Receptors, Atrial Natriuretic Factor - genetics | Adenylate Cyclase Toxin - metabolism | Enzyme Activation | Kinetics | Antigens, Bacterial - metabolism | Receptors, Cytoplasmic and Nuclear - metabolism | Whooping-cough | Dropsy | Edema | Pyrimidines | Analysis | Nitric oxide | Pyrimidine nucleotides | Physiological aspects | Natriuretic peptides | Membranes | GTP | Physiological effects | Peptides | Sperm | Nucleotides | Rod outer segment membranes | Kinases | Guanylate cyclase | Medical schools | Proteins | Pertussis | Cell growth | Chloride | Substrate specificity | Rodents | Bacteria | Physiology | Catalysis | Chemical synthesis | Adenosine triphosphate | Medical research | Particulates | Pharmacology | Liquid chromatography | High-performance liquid chromatography | Substrates | Exotoxins | Active sites | Scientific imaging | Toxins | Mass spectrometry | CTP | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 07/2004, Volume 430, Issue 6997, pp. 317 - 322
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2010, Volume 107, Issue 49, pp. 21193 - 21198
Journal Article