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1. Full Text Successful fertility outcome in a woman with 17ɑ‐hydroxylase deficiency
by Falhammar, Henrik
Clinical Endocrinology, ISSN 0300-0664, 04/2018, Volume 88, Issue 4, pp. 607 - 609
Hydroxylase
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2. Full Text Effect of a single and repeated stress exposure on gene expression of catecholamine biosynthetic enzymes in brainstem catecholaminergic cell groups in rats
by Mravec, Boris and Vargovic, Peter and Filipcik, Peter and Novak, Michal and Kvetnansky, Richard
European Journal of Neuroscience, ISSN 0953-816X, 07/2015, Volume 42, Issue 2, pp. 1872 - 1886
Brainstem catecholaminergic neurons significantly participate in the regulation of neuroendocrine system activity, particularly during stressful conditions.... 
mRNA | immobilisation stress | tyrosine hydroxylase protein | dopamine‐β‐hydroxylase | phenylethanolamine N‐methyltransferase | tyrosine hydroxylase | Tyrosine hydroxylase protein | Immobilisation stress | Dopamine-β-hydroxylase mRNA | Phenylethanolamine N-methyltransferase mRNA | Tyrosine hydroxylase mRNA | ACTIVATION | TYROSINE-HYDROXYLASE | tyrosine hydroxylase mRNA | IMMOBILIZATION STRESS | FUNCTIONAL NEUROANATOMY | phenylethanolamine N-methyltransferase mRNA | NEUROSCIENCES | HYPOTHALAMIC PARAVENTRICULAR NUCLEUS | HYDROXYLASE MESSENGER-RNA | STELLATE GANGLIA | dopamine-beta-hydroxylase mRNA | NEURONS | NORADRENERGIC LOCUS-COERULEUS | SYMPATHETIC-GANGLIA | Immobility Response, Tonic - physiology | Tyrosine 3-Monooxygenase - metabolism | Catecholamines - metabolism | Microdissection | Brain Stem - metabolism | Rats | Male | Gene Expression Regulation, Enzymologic - physiology | RNA, Messenger - metabolism | Rats, Sprague-Dawley | Tyrosine 3-Monooxygenase - genetics | Animals | Time Factors | Dopamine beta-Hydroxylase - genetics | Dopamine beta-Hydroxylase - metabolism | Phenylethanolamine N-Methyltransferase - metabolism | Phenylethanolamine N-Methyltransferase - genetics | Index Medicus
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3. Full Text Activation of farnesoid X receptor prevents atherosclerotic lesion formation in LDLR-/- and apoE -/- mice
by Hartman, Helen B and Gardell, Stephen J and Petucci, Chris J and Wang, Shuguang and Krueger, Julie A and Evans, Mark J
Journal of Lipid Research, ISSN 0022-2275, 06/2009, Volume 50, Issue 6, pp. 1090 - 1100
The role of farnesoid X receptor (FXR) in the development of atherosclerosis has been unclear. Here, LDL receptor (LDLR-/-) or apolipoprotein E (apoE(-/-))... 
Cholesterol 7α-hydroxylase | Sterol 12 α-hydroxylase | Atherosclerosis | Small heterodimer partner | atherosclerosis | TRIGLYCERIDE LEVELS | TRANSGENIC EXPRESSION | NEGATIVE FEEDBACK-REGULATION | NUCLEAR RECEPTORS | BIOCHEMISTRY & MOLECULAR BIOLOGY | BILE-ACID SYNTHESIS | ESTROGEN-RECEPTOR | DENSITY-LIPOPROTEIN CHOLESTEROL | cholesterol 7 alpha-hydroxylase | NONFASTING TRIGLYCERIDES | small heterodimer partner | E-DEFICIENT MICE | sterol 12 alpha-hydroxylase | Dyslipidemias - genetics | Apolipoproteins E - deficiency | Gene Expression - drug effects | Steroid 12-alpha-Hydroxylase - antagonists & inhibitors | Receptors, Cytoplasmic and Nuclear - deficiency | Atherosclerosis - genetics | Male | Lipids - blood | Receptors, LDL - deficiency | Dyslipidemias - prevention & control | Female | Indoles - pharmacology | Receptors, LDL - genetics | Atherosclerosis - pathology | Mice, Inbred C57BL | Bile Acids and Salts - metabolism | Receptors, Cytoplasmic and Nuclear - agonists | Receptors, Cytoplasmic and Nuclear - genetics | Atherosclerosis - metabolism | Mice, Knockout | Azepines - pharmacology | Cholesterol 7-alpha-Hydroxylase - genetics | Steroid 12-alpha-Hydroxylase - genetics | Animals | Apolipoproteins E - genetics | Receptors, Cytoplasmic and Nuclear - antagonists & inhibitors | Dyslipidemias - metabolism | Mice | Cholesterol 7-alpha-Hydroxylase - antagonists & inhibitors | Atherosclerosis - prevention & control | Receptors, Cytoplasmic and Nuclear - metabolism | Index Medicus | sterol 12 α-hydroxylase | cholesterol 7α-hydroxylase
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4. Full Text Development of monoclonal antibodies against human CYP11B1 and CYP11B2
by Gomez-Sanchez, Celso E and Gomez-Sanchez, Elise P and Qi, Xin and Velarde-Miranda, Carolina and Plonczynski, Maria W and Parker, C. Richard and Rainey, William and Satoh, Fumitoshi and Maekawa, Takashi and Nakamura, Yasuhiro and Sasano, Hironobu
Molecular and Cellular Endocrinology, ISSN 0303-7207, 03/2014, Volume 383, Issue 1-2, pp. 111 - 117
1.The final enzymes in the biosynthesis of aldosterone and cortisol are by the cytochrome P450 CYP11B2 and CYP11B1, respectively. The enzymes are 93%... 
Monoclonal antibodies | Immunofluorescence | CYP11B2 | CYP11B1 | Adrenal cortex | 17α-Hydroxylase | 17 alpha-Hydroxylase | lmmunofluorescence | DIAGNOSIS | MESSENGER-RNA EXPRESSION | HYPERPLASIA | PARTIAL ALDOSTERONE RESISTANCE | CELL BIOLOGY | SYNTHASE | RAT ADRENAL-CORTEX | GENE | ZONA GLOMERULOSA | BIOSYNTHESIS | ENDOCRINOLOGY & METABOLISM | ADENOMA | Antibodies, Monoclonal - biosynthesis | Humans | Steroid 11-beta-Hydroxylase - immunology | Molecular Sequence Data | Peptides - administration & dosage | Peptides - chemical synthesis | Zona Fasciculata - immunology | Steroid 17-alpha-Hydroxylase - immunology | Adult | Cytochrome P-450 CYP11B2 - metabolism | Infant, Newborn | Amino Acid Sequence | Zona Glomerulosa - ultrastructure | Peptides - immunology | Rats | Zona Glomerulosa - metabolism | Antibodies, Monoclonal - isolation & purification | Immunohistochemistry - methods | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Steroid 11-beta-Hydroxylase - metabolism | Cytochrome P-450 CYP11B2 - immunology | Zona Glomerulosa - immunology | Zona Fasciculata - metabolism | Mice | Steroid 17-alpha-Hydroxylase - metabolism | Zona Fasciculata - ultrastructure | Cytochrome P-450 | Index Medicus
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5. Full Text Dysregulation of renal vitamin D metabolism in the uremic rat
by Helvig, Christian F and Cuerrier, Dominic and Hosfield, Christopher M and Ireland, Breanna and Kharebov, Aza Z and Kim, Jae W and Ramjit, Navindra J and Ryder, Kara and Tabash, Samir P and Herzenberg, Andrew M and Epps, Tina M and Petkovich, Martin
Kidney International, ISSN 0085-2538, 09/2010, Volume 78, Issue 5, pp. 463 - 472
The progressive decline in kidney function and concomitant loss of renal 1α-hydroxylase (CYP27B1) in chronic kidney disease (CKD) are associated with a gradual... 
chronic kidney disease | 24-hydroxylase | adenine rat model | vitamin D metabolites | 1α-hydroxylase | 25-HYDROXYVITAMIN D-3-1-ALPHA-HYDROXYLASE | SECONDARY HYPERPARATHYROIDISM | LINKED HYPOPHOSPHATEMIC RICKETS | MESSENGER-RNA | PHOSPHATE HOMEOSTASIS | 1 alpha-hydroxylase | PROSTATE-CANCER CELLS | 24,25-DIHYDROXYVITAMIN D | UROLOGY & NEPHROLOGY | 1,25-DIHYDROXYVITAMIN D-3 | CANDIDATE ONCOGENE | CHRONIC KIDNEY-DISEASE | Immunohistochemistry | 25-Hydroxyvitamin D3 1-alpha-Hydroxylase - analysis | 25-Hydroxyvitamin D3 1-alpha-Hydroxylase - genetics | RNA, Messenger - analysis | Rats | Male | Vitamin D3 24-Hydroxylase | Steroid Hydroxylases - analysis | Uremia - metabolism | Rats, Sprague-Dawley | Kidney - metabolism | Animals | Calcitriol - pharmacology | Vitamin D - metabolism | Steroid Hydroxylases - genetics | Index Medicus
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6. Cholesterol 7 [alpha]-hydroxylase (7 [alphamonooxygenase)
by Fears, Robin and Sabine, John R and Fears, R
1986, ISBN 9780849365539, 204
Cholesterol hydroxylase | Bile acids | Metabolism | Cholesterol
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7. Full Text Differential response of the central noradrenergic nervous system to the loss of locus coeruleus neurons in Parkinson's disease and Alzheimer's disease
by McMillan, Pamela J and White, Sylvia S and Franklin, Allyn and Greenup, J. Lynne and Leverenz, James B and Raskind, Murray A and Szot, Patricia
Brain Research, ISSN 0006-8993, 2010, Volume 1373, pp. 240 - 252
Abstract In Parkinson's disease (PD), there is a significant loss of noradrenergic neurons in the locus coeruleus (LC) in addition to the loss of dopaminergic... 
Neurology | Immunohistochemistry | Parkinson's disease | Tyrosine hydroxylase | Norepinephrine transporter | mRNA | Alzheimer's disease | Locus coeruleus | Dopamine β-hydroxylase | TYROSINE-HYDROXYLASE | DOPAMINE-BETA-HYDROXYLASE | LESIONED PRIMATE MODEL | CELL LOSS | SUBSTANTIA-NIGRA | NEUROSCIENCES | Dopamine beta-hydroxylase | STRIATAL DOPAMINE | TRANSPORTER MESSENGER-RNA | INDUCED DYSKINESIAS | LEWY BODIES | Tyrosine 3-Monooxygenase - metabolism | Parkinson Disease - pathology | Fluoxetine - pharmacokinetics | Humans | Locus Coeruleus - pathology | Middle Aged | Male | RNA, Messenger - metabolism | Alzheimer Disease - pathology | Tyrosine 3-Monooxygenase - genetics | Cell Count - methods | Dopamine beta-Hydroxylase - genetics | Fluoxetine - analogs & derivatives | Protein Binding - drug effects | Binding Sites - physiology | Dopamine beta-Hydroxylase - metabolism | Neurons - physiology | Aged, 80 and over | Female | Aged | Norepinephrine Plasma Membrane Transport Proteins - metabolism | Binding Sites - drug effects | Tritium - pharmacokinetics | Index Medicus | norepinephrine transporter | dopamine β-hydroxylase | immunohistochemistry | locus coeruleus | tyrosine hydroxylase
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8. Full Text Involvement of Corepressor Complex Subunit GPS2 in Transcriptional Pathways Governing Human Bile Acid Biosynthesis
by Sabyasachi Sanyal and Ann Båvner and Anna Haroniti and Lisa-Mari Nilsson and Thomas Lundåsen and Stefan Rehnmark and Michael Robin Witt and Curt Einarsson and Iannis Talianidis and Jan-Åke Gustafsson and Eckardt Treuter
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2007, Volume 104, Issue 40, pp. 15665 - 15670
Coordinated regulation of bile acid biosynthesis, the predominant pathway for hepatic cholesterol catabolism, is mediated by few key nuclear receptors... 
Hep G2 cells | Receptors | Messenger RNA | Bile acids | Hepatocytes | Small interfering RNA | Gene expression regulation | Biosynthesis | Promoter regions | Repression | Farnesoid X receptor | Sterol 12α hydroxylase | Cholesterol 7α hydroxylase | Small heterodimer partner | FXR | farnesoid X receptor | NEGATIVE FEEDBACK-REGULATION | MULTIDISCIPLINARY SCIENCES | IDENTIFICATION | ORPHAN NUCLEAR RECEPTOR | cholesterol 7 alpha hydroxylase | REPRESSION | GENE | TRANSACTIVATION | sterol 12 alpha hydroxylase | LIVER | small heterodimer partner | SHP | Steroid 12-alpha-Hydroxylase - metabolism | Promoter Regions, Genetic | Humans | Bile Acids and Salts - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Receptors, Cytoplasmic and Nuclear - genetics | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Liver Neoplasms | DNA-Binding Proteins - metabolism | Gene Expression Regulation, Enzymologic | Transcription Factors - metabolism | Cholesterol 7-alpha-Hydroxylase - genetics | Steroid 12-alpha-Hydroxylase - genetics | Cholesterol 7-alpha-Hydroxylase - metabolism | Cell Line, Tumor | Transcription, Genetic | Carcinoma, Hepatocellular | Receptors, Cytoplasmic and Nuclear - metabolism | Research | Genetic transcription | Hydroxylases | Properties | Observations | Amino acids | Biochemistry | T cell receptors | Gene expression | Cells | Cholesterol | Index Medicus | Biological Sciences | sterol 12α hydroxylase | cholesterol 7α hydroxylase
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9. Full Text Congenital adrenal hyperplasia due to 11-hydroxylase deficiency—Compound heterozygous mutations of a prevalent and two novel CYP11B1 mutations
by Gu, Chongjuan and Tan, Hao and Yang, Junbao and Lu, Yilu and Ma, Yongxin
Gene, ISSN 0378-1119, 08/2017, Volume 626, pp. 89 - 94
11β-hydroxylase deficiency (11β-OHD) occurs in about 5–8% of congenital adrenal hyperplasia (CAH). In this study, we identified three (encoding Cytochrome P450... 
Congenital adrenal hyperplasia | Mutation | CYP11B1 | 11β-hydroxylase deficiency | 11-BETA-HYDROXYLASE DEFICIENCY | FUNCTIONAL CONSEQUENCES | FAMILY | SWISS-MODEL | VARIABILITY | 11 beta-hydroxylase deficiency | GENE | SERVER | GENETICS & HEREDITY | BETA-HYDROXYLASE DEFICIENCY | CHINESE PATIENTS | INSIGHTS | Heme - metabolism | Humans | Male | Adrenal Hyperplasia, Congenital - genetics | Mutation, Missense | Steroid 11-beta-Hydroxylase - genetics | Cortodoxone - metabolism | Steroid 11-beta-Hydroxylase - metabolism | Steroid 11-beta-Hydroxylase - chemistry | Pedigree | Adrenal Hyperplasia, Congenital - diagnosis | HEK293 Cells | Protein Binding | Adult | Female | Heterozygote | Binding Sites | Proteins | Genetic disorders | Corticosteroids | Analysis | Heme | Adrenogenital syndrome | Cytochrome P-450 | Genetic aspects | Medical genetics | Intermedin | Index Medicus
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10. Phenylalanine hydroxylase misfolding and pharmacological chaperones
by Underhaug, Jarl and Aubi, Oscar and Martinez, Aurora
Current Topics in Medicinal Chemistry, ISSN 1568-0266, 2012, Volume 12, Issue 22, pp. 2534 - 2545
Phenylketonuria (PKU) is a loss-of-function inborn error of metabolism. As many other inherited diseases the main pathologic mechanism in PKU is an enhanced... 
High-throughput screening | Pharmacophore modeling | Pharmachaperones | Phenylalanine hydroxylase | Folding aids | CHEMISTRY, MEDICINAL | TYROSINE-HYDROXYLASE | MOLECULAR CHAPERONES | CRYSTAL-STRUCTURE | high-throughput screening | DRUG DISCOVERY | THERMAL SHIFT ASSAYS | folding aids | STRUCTURAL BASIS | TRYPTOPHAN-HYDROXYLASE | MOUSE MODEL | pharmacophore modeling | AMINO-ACID HYDROXYLASES | SURFACE-PLASMON RESONANCE | pharmachaperones | Phenylalanine Hydroxylase - genetics | Phenylketonurias - enzymology | Tyrosine 3-Monooxygenase - metabolism | Molecular Chaperones - metabolism | Humans | Biopterin - analogs & derivatives | Protein Folding | Biopterin - metabolism | Animals | Mice | Binding Sites | Molecular Targeted Therapy - methods | Phenylalanine Hydroxylase - chemistry | Phenylalanine Hydroxylase - metabolism | Disease Models, Animal | High-Throughput Screening Assays - methods | Molecular Chaperones - pharmacology | Phenylketonurias - drug therapy | Precision Medicine
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11. Full Text Autoantibodies against aromatic amino acid hydroxylases in patients with autoimmune polyendocrine syndrome type 1 target multiple antigenic determinants and reveal regulatory regions crucial for enzymatic activity
by Bratland, Eirik and Magitta, Ng’weina Francis and Bøe Wolff, Anette Susanne and Ekern, Trude and Knappskog, Per Morten and Kämpe, Olle and Haavik, Jan and Husebye, Eystein Sverre and Medicinska fakulteten and Medicinska och farmaceutiska vetenskapsområdet and Uppsala universitet and Institutionen för medicinska vetenskaper and Autoimmunitet
Immunobiology, ISSN 0171-2985, 2012, Volume 218, Issue 6, pp. 899 - 909
Abstract Patients with autoimmune polyendocrine syndrome type 1 (APS-1) frequently have autoantibodies directed against the aromatic amino acid hydroxylases... 
Allergy and Immunology | Advanced Basic Science | Tryptophan hydroxylase | Aromatic amino acid hydroxylases | Tyrosine hydroxylase | Autoimmune polyendocrine syndrome type 1 | Aire | PROTEIN | SPECIFICITY | HUMAN TRYPTOPHAN-HYDROXYLASE | IMMUNOLOGY | HUMAN PHENYLALANINE-HYDROXYLASE | CANDIDIASIS-ECTODERMAL DYSTROPHY | SYNDROME TYPE-I | GENE | SEROTONIN | HUMAN TYROSINE-HYDROXYLASE | T-CELLS | Tyrosine 3-Monooxygenase - metabolism | Epitopes - metabolism | Autoantibodies - blood | Humans | Molecular Sequence Data | Immunoblotting | Isoenzymes - immunology | Epitopes - immunology | Sweden | Tyrosine 3-Monooxygenase - immunology | Antibody Specificity - immunology | Isoenzymes - metabolism | Binding Sites - immunology | Tryptophan Hydroxylase - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Biocatalysis | Isoenzymes - genetics | Models, Molecular | Binding Sites - genetics | Polyendocrinopathies, Autoimmune - blood | Polyendocrinopathies, Autoimmune - immunology | Tryptophan Hydroxylase - genetics | Tyrosine 3-Monooxygenase - genetics | Autoantibodies - immunology | Norway | Tryptophan Hydroxylase - immunology | Finland | Denmark | Epitopes - chemistry | Polyendocrinopathies, Autoimmune - enzymology | Cohort Studies | Autoimmunity | Care and treatment | Autoantibodies | Phenylalanine | Mycoses | Tryptophan | Hydroxylases | Glutamate | Antigenic determinants | Index Medicus | Medical and Health Sciences | Medicin och hälsovetenskap
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12. Full Text Tetrahydrobiopterin treatment reduces brain L-Phe but only partially improves serotonin in hyperphenylalaninemic ENU1/2 mice
by Scherer, Tanja and Allegri, Gabriella and Sarkissian, Christineh N and Ying, Ming and Grisch-Chan, Hiu Man and Rassi, Anahita and Winn, Shelley R and Harding, Cary O and Martinez, Aurora and Thöny, Beat
Journal of Inherited Metabolic Disease, ISSN 0141-8955, 7/2018, Volume 41, Issue 4, pp. 709 - 718
Hyperphenylalaninemia (HPA) caused by hepatic phenylalanine hydroxylase (PAH) deficiency has severe consequences on brain monoamine neurotransmitter... 
Human Genetics | Biochemistry, general | Pediatrics | Monoamine neurotransmitter | Medicine & Public Health | Tryptophan hydroxylase 2 | Metabolic Diseases | Internal Medicine | Tyrosine hydroxylase | GTP cyclohydrolase (GTPCH) and GTP cyclohydrolase feedback-regulatory protein (GFRP) | MEDICINE, RESEARCH & EXPERIMENTAL | TYROSINE-HYDROXYLASE | PHENYLKETONURIA | PATHOGENESIS | BIOSYNTHESIS | ENDOCRINOLOGY & METABOLISM | GENETICS & HEREDITY | DYSFUNCTION | MUTATIONS | GENETIC MOUSE MODEL | FEEDBACK REGULATORY PROTEIN | EXPRESSION | PHENYLALANINE-HYDROXYLASE DEFICIENCY | Serotonin | Analysis | Depression, Mental | Physiological aspects | Phenols | Amino acids | Hydroxylases | Blood proteins | Tyrosine | GTP | Phenylalanine 4-monooxygenase | Phenylalanine | Hydroxylase | Liver | Dietary supplements | Tryptophan | Mental depression | Tyrosine 3-monooxygenase | Tryptophan hydroxylase | Proteins | Mood | GTP cyclohydrolase | Tetrahydrobiopterin | L-Tryptophan | Anxiety | Supplementation | GTP cyclohydrolase feedback-regulatory protein (GFRP) | GTP cyclohydrolase (GTPCH)
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