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1. Full Text Separation of turkey lactate dehydrogenase isoenzymes using isoelectric focusing technique
by Heinová, Dagmar and Kostecká, Zuzana and Csank, Tomáš
ELECTROPHORESIS, ISSN 0173-0835, 01/2016, Volume 37, Issue 2, pp. 335 - 338
Native polyacrylamide gel electrophoresis at pH 8.8 did not allow to separate lactate dehydrogenase (LDH) isoenzymes of turkey origin. Five electrophoretically... 
Birds | Turkey | Isoelectric focusing | Mammals | Lactate dehydrogenase isoenzymes | CHEMISTRY, ANALYTICAL | EVOLUTIONARY RELATIONSHIPS | BACTERIA | SEQUENCES | BIOCHEMICAL RESEARCH METHODS | BREAST MUSCLE | PATTERNS | LDH | ENZYME | TISSUES | CREATINE-KINASE | Turkeys - metabolism | Liver - enzymology | Kidney - enzymology | Brain - enzymology | L-Lactate Dehydrogenase - isolation & purification | Isoenzymes - isolation & purification | Lung - enzymology | Myocardium - enzymology | Animals | Spleen - enzymology | Isoelectric Focusing - methods | Erythrocytes - enzymology | Pancreas - enzymology | Lactate dehydrogenase | Methods | Kidneys | Breast | Muscles | Electrophoresis | Serums
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2. Full Text Ceramide synthase 5 is essential to maintain C16:0-Ceramide pools and contributes to the development of diet-induced obesity
by Gosejacob, Dominic and Jäger, Philipp S and Dorp, Katharina Vom and Frejno, Martin and Carstensen, Anne C and Köhnke, Monika and Degen, Joachim and Dörmann, Peter and Hoch, Michael
Journal of Biological Chemistry, ISSN 0021-9258, 03/2016, Volume 291, Issue 13, pp. 6989 - 7003
Ceramides are bioactive sphingolipids, which are composed of sphingoid bases carrying acyl chains of various lengths. Ceramides are synthesized by a family of... 
Liver - pathology | Liver - enzymology | Male | Obesity - genetics | Ceramides - biosynthesis | Lung - enzymology | Spleen - enzymology | Diet, High-Fat | Obesity - etiology | Spleen - pathology | Adipose Tissue, White - pathology | Dietary Fats - adverse effects | Gene Expression | Glucose Tolerance Test | Lung - pathology | Muscle, Skeletal - enzymology | Isoenzymes - genetics | Sphingosine N-Acyltransferase - deficiency | Mice, Inbred C57BL | Isoenzymes - deficiency | Mice, Knockout | Obesity - pathology | Animals | Sphingosine N-Acyltransferase - genetics | Adipose Tissue, White - enzymology | Insulin Resistance - genetics | Mice | Obesity - enzymology | Muscle, Skeletal - pathology | Blood Glucose - metabolism | gene knockout | ceramide | adipose tissue metabolism | sphingolipid | lipid metabolism | ceramide synthase | Lipids | metabolism | diabetes | insulin resistance | obesity
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3. Full Text Caspase-1, Caspase-8, and Calpain Are Dispensable for IL-33 Release by Macrophages
by Ohno, Tatsukuni and Oboki, Keisuke and Kajiwara, Naoki and Morii, Eiichi and Aozasa, Katsuyuki and Flavell, Richard A and Okumura, Ko and Saito, Hirohisa and Nakae, Susumu
The Journal of Immunology, ISSN 0022-1767, 12/2009, Volume 183, Issue 12, pp. 7890 - 7897
In addition to IL-1 and IL-18, IL-33 was recently identified as a member of the IL-1 cytokine family. rIL-33 can promote production of Th2-type cytokines by... 
ST2 | TH2 CELLS | IL-18 | RECEPTOR | CYTOKINE | LIGAND | IMMUNOLOGY | HUMAN MAST-CELLS | MATURATION | INTERLEUKIN-1-BETA CONVERTING-ENZYME | ANTIGEN | Hypersensitivity - enzymology | Spleen - immunology | Bone Marrow Cells - enzymology | Dendritic Cells - immunology | Macrophages, Peritoneal - pathology | Hypersensitivity - immunology | Bone Marrow Cells - secretion | Calpain - physiology | Interleukins - physiology | Spleen - enzymology | Bone Marrow Cells - immunology | Caspase 1 - physiology | Inflammation Mediators - physiology | Mast Cells - immunology | Interleukin-33 | Cells, Cultured | Macrophages, Peritoneal - enzymology | Macrophages, Peritoneal - immunology | Spleen - cytology | Caspase 8 - physiology | Macrophages, Peritoneal - secretion | Mast Cells - enzymology | Mice, Knockout | Dendritic Cells - secretion | Animals | Dendritic Cells - enzymology | Hypersensitivity - pathology | Mast Cells - secretion | Mice | Mice, Inbred BALB C | Interleukins - secretion
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4. Full Text Regulation of intracellular levels of NAD: A novel role for CD38
by Aksoy, Pinar and White, Thomas A and Thompson, Michael and Chini, Eduardo N
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 2006, Volume 345, Issue 4, pp. 1386 - 1392
Nicotinamide adenine dinucleotide (NAD) plays key roles in many cellular functions. In addition to its well-known role in energy metabolism, NAD also plays a... 
NAD | Brain | CD38 | cADPR | Calcium | CYCLASE | CYCLIC ADP-RIBOSE | calcium | ADENINE-DINUCLEOTIDE PHOSPHATE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SEA-URCHIN EGGS | ENZYMATIC-SYNTHESIS | brain | IDENTIFICATION | NAADP | BIOPHYSICS | CALCIUM-RELEASE | MICE | GLYCOHYDROLASE | Mitochondria - enzymology | Testis - metabolism | NAD+ Nucleosidase - metabolism | Humans | ADP-ribosyl Cyclase 1 - physiology | Brain - enzymology | Male | Cell Nucleus - enzymology | Brain - metabolism | Cell Nucleus - metabolism | Spleen - enzymology | Myocardium - metabolism | Testis - enzymology | Female | Cell Membrane - metabolism | Catalysis | Intracellular Fluid - metabolism | NAD - metabolism | ADP-ribosyl Cyclase 1 - genetics | Mice, Inbred C57BL | Cells, Cultured | Genotype | Mitochondria - metabolism | Blotting, Western | Mice, Knockout | Cell Membrane - enzymology | Myocardium - enzymology | Animals | Spleen - metabolism | ADP-ribosyl Cyclase 1 - metabolism | Mice | Hydrolysis | Niacinamide | Cell research | Physiological aspects | Adenine | NAD (Coenzyme) | Mitochondrial DNA
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5. Full Text Differential Lysosomal Proteolysis in Antigen-Presenting Cells Determines Antigen Fate
by Lélia Delamarre and Margit Pack and Henry Chang and Ira Mellman and E. Sergio Trombetta
Science, ISSN 0036-8075, 3/2005, Volume 307, Issue 5715, pp. 1630 - 1634
Antigen-presenting cells (APCs) internalize antigens and present antigen-derived peptides to T cells. Although APCs have been thought to exhibit a... 
Spleen | T lymphocytes | Antigens | Dextrans | Plant growth regulators | B lymphocytes | Lysosomes | Reports | Biosynthesis | Ova | Lymph nodes | Lymphoid Tissue - enzymology | Membrane Glycoproteins - metabolism | Dendritic Cells - immunology | Lysosomes - enzymology | Ribonucleases - metabolism | Lymphoid Tissue - immunology | Endocytosis | Antigen Presentation | Ribonuclease, Pancreatic - immunology | Horseradish Peroxidase - immunology | Lysosome-Associated Membrane Glycoproteins | B-Lymphocytes - metabolism | Dendritic Cells - metabolism | Macrophages - immunology | Peptide Hydrolases - metabolism | Green Fluorescent Proteins - metabolism | Antigen-Presenting Cells - metabolism | B-Lymphocytes - enzymology | Cells, Cultured | Antigens - metabolism | Antigen-Presenting Cells - immunology | Mice, Inbred C3H | Macrophages - enzymology | Lysosomes - ultrastructure | Lymphoid Tissue - cytology | Macrophages - metabolism | Animals | B-Lymphocytes - immunology | Green Fluorescent Proteins - immunology | Histocompatibility Antigens Class II - immunology | Ribonuclease, Pancreatic - metabolism | Dendritic Cells - enzymology | Ribonucleases - immunology | Horseradish Peroxidase - metabolism | Mice | Antigen-Presenting Cells - enzymology | Antigen presenting cells | Research | Proteolysis | Proteins | Antigen presentation
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6. Full Text Randomized, controlled trial of miglustat in Gaucher's disease type 3
by Schiffmann, Raphael and Fitzgibbon, Edmond J and Harris, Chris and DeVile, Catherine and Davies, Elin H and Abel, Larry and van Schaik, Ivo N and Benko, William and Timmons, Margaret and Ries, Markus and Vellodi, Ashok
Annals of neurology, ISSN 0364-5134, 2008, Volume 64, Issue 5, pp. 514 - 522
To evaluate the efficacy and safety of miglustat, concomitant with enzyme replacement therapy (ERT), in patients with Gaucher's disease type 3 (GD3). This... 
EFFICACY | BIOSYNTHESIS | OGT-918 | INVOLVEMENT | IDENTIFICATION | INHIBITOR | ENZYME REPLACEMENT THERAPY | NEUROSCIENCES | N-BUTYLDEOXYNOJIRIMYCIN | CLINICAL NEUROLOGY | Liver - enzymology | Ocular Motility Disorders - enzymology | Humans | Child, Preschool | Male | Spleen - drug effects | Lung Diseases - drug therapy | Lung - enzymology | Enzyme Inhibitors - administration & dosage | Young Adult | Hexosaminidases - metabolism | Liver - drug effects | Spleen - enzymology | Endpoint Determination | 1-Deoxynojirimycin - administration & dosage | 1-Deoxynojirimycin - analogs & derivatives | Female | Gaucher Disease - physiopathology | Saccades - physiology | Child | Gaucher Disease - drug therapy | Gaucher Disease - enzymology | Lung Diseases - enzymology | Treatment Outcome | Glucosylceramidase - metabolism | Ocular Motility Disorders - drug therapy | Lung - drug effects | Adolescent | Ocular Motility Disorders - physiopathology | Saccades - drug effects
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7. Full Text Tissue Transglutaminase contributes to experimental multiple sclerosis pathogenesis and clinical outcome by promoting macrophage migration
by van Strien, Miriam E and de Vries, Helga E and Chrobok, Navina L and Bol, John G.J.M and Breve, John J.P and van der Pol, Susanne M.P and Kooij, Gijs and van Buul, Jaap D and Karpuj, Marcela and Steinman, Lawrence and Wilhelmus, Micha M and Sestito, Claudia and Drukarch, Benjamin and Van Dam, Anne-Marie
Brain, Behavior, and Immunity, ISSN 0889-1591, 2015, Volume 50, pp. 141 - 154
Highlights • TG2 is present in MHCII+ infiltrating cells in active MS lesions. • Inhibition of TG2 activity dramatically reduces clinical symptoms of EAE. •... 
Psychiatry | Allergy and Immunology | Immunohistochemistry | Experimental autoimmune encephalomyelitis | Multiple sclerosis | Demyelination | Migration | encephalomyelitis | EXPERIMENTAL AUTOIMMUNE ENCEPHALOMYELITIS | DIFFERENTIAL EXPRESSION | TRANSENDOTHELIAL MIGRATION | ALZHEIMERS-DISEASE | EXPERIMENTAL ALLERGIC ENCEPHALOMYELITIS | CROSS-LINKING | IMMUNOLOGY | NEUROSCIENCES | LESIONS | NITRIC-OXIDE | SELECTIVE INHIBITORS | Experimental autoimmune | CENTRAL-NERVOUS-SYSTEM | GTP-Binding Proteins - antagonists & inhibitors | Humans | Cerebral Cortex - pathology | Transglutaminases - genetics | Male | RNA, Messenger - metabolism | GTP-Binding Proteins - genetics | T-Lymphocytes - metabolism | Spinal Cord - pathology | Inflammation Mediators - metabolism | Aged, 80 and over | Female | Myelin Sheath - enzymology | Transglutaminases - antagonists & inhibitors | Cerebral Cortex - enzymology | Multiple Sclerosis - enzymology | Encephalomyelitis, Autoimmune, Experimental - pathology | Mice, Inbred C57BL | Spinal Cord - enzymology | Rats | Macrophages - enzymology | Mice, Knockout | Isoxazoles - pharmacology | Cell Movement - drug effects | Animals | Encephalomyelitis, Autoimmune, Experimental - enzymology | Spleen - metabolism | Transglutaminases - metabolism | Multiple Sclerosis - pathology | Aged | Mice | Endothelial Cells - pathology | Endothelial Cells - enzymology | GTP-Binding Proteins - metabolism | T cells | Macrophages | Patient outcomes
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8. Full Text Nuclear and cytoplasmic AID in extrafollicular and germinal center B cells
by Cattoretti, Giorgio and Büttner, Maike and Shaknovich, Rita and Kremmer, Elisabeth and Alobeid, Bachir and Niedobitek, Gerald
Blood, ISSN 0006-4971, 05/2006, Volume 107, Issue 10, pp. 3967 - 3975
Activation-induced cytidine deaminase (AID) is necessary for immunoglobulin somatic hypermutation (SHM) and class switch recombination (CSR) in T-dependent... 
ACTIVATION-INDUCED DEAMINASE | IMMUNE-RESPONSE | CLASS SWITCH RECOMBINATION | AVIDIN-BINDING ACTIVITY | SOMATIC HYPERMUTATION | INDUCED CYTIDINE DEAMINASE | GENE-EXPRESSION | MONOCLONAL-ANTIBODY | LYMPHOID-CELLS | HEMATOLOGY | NF-KAPPA-B | Cytoplasm - enzymology | Rabbits | B-Lymphocytes - enzymology | Goats | Humans | Rats | Cell Nucleus - enzymology | Lymph Nodes - enzymology | Animals | Spleen - enzymology | Cytidine Deaminase - metabolism | Mice | Enzyme Activation | Palatine Tonsil - enzymology
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9. Full Text Eliglustat maintains long-term clinical stability in patients with Gaucher disease type 1 stabilized on enzyme therapy
by Cox, Timothy M and Drelichman, Guillermo and Cravo, Renata and Balwani, Manisha and Burrow, Thomas Andrew and Martins, Ana Maria and Lukina, Elena and Rosenbloom, Barry and Goker-Alpan, Ozlem and Watman, Nora and El-Beshlawy, Amal and Kishnani, Priya S and Pedroso, Maria Lucia and Gaemers, Sebastiaan J.M and Tayag, Regina and Peterschmitt, M. Judith
Blood, ISSN 0006-4971, 04/2017, Volume 129, Issue 17, pp. 2375 - 2383
In the phase 3 Study of Eliglustat Tartrate (Genz-112638) in Patients With Gaucher Disease Who Have Reached Therapeutic Goals With Enzyme Replacement Therapy... 
NON-INFERIORITY | TRIAL | DIAGNOSIS | MANAGEMENT | RECOMMENDATIONS | REPLACEMENT THERAPY | ADULTS | OPEN-LABEL | HEMATOLOGY | ORAL ELIGLUSTAT | IMIGLUCERASE | Recombinant Proteins - therapeutic use | Enzyme Replacement Therapy | Liver - enzymology | Administration, Oral | Humans | Middle Aged | Femur - drug effects | Male | Lumbar Vertebrae - drug effects | Spleen - drug effects | Enzyme Inhibitors - therapeutic use | Pyrrolidines - therapeutic use | Bone Density - drug effects | Platelet Count | Liver - drug effects | Spleen - enzymology | Femur - enzymology | Glucosylceramidase - therapeutic use | Adult | Female | Gaucher Disease - physiopathology | Gaucher Disease - drug therapy | Gaucher Disease - enzymology | Lumbar Vertebrae - enzymology | 100 | Clinical Trials and Observations | 101
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10. Full Text The role of Janus Kinase 2 V617F mutation in extramedullary hematopoiesis of the spleen in neoplastic myeloid disorders
by Hsieh, Pin-Pen and Olsen, Randy J and O'Malley, Dennis P and Konoplev, Sergej N and Hussong, Jerry W and Dunphy, Cherie H and Perkins, Sherrie L and Cheng, Liang and Lin, Pei and Chang, Chung-Che
Modern Pathology, ISSN 0893-3952, 09/2007, Volume 20, Issue 9, pp. 929 - 935
Extramedullary hematopoiesis ( EMH) in the spleen is a characteristic feature of the chronic myeloproliferative disorders ( CMPDs) and various other neoplastic... 
JAK2 | Chronic myeloproliferative disorders | Extramedullary hematopoiesis | MYELOFIBROSIS | JAK2(V617F) | POLYCYTHEMIA-VERA | JAK2(V617F) MUTATION | JAK2 V617F | chronic myeloproliferative disorders | MYELODYSPLASTIC-SYNDROMES | PATHOLOGY | ESSENTIAL THROMBOCYTHEMIA | extramedullary hematopoiesis | ACTIVATING MUTATION | ACUTE LYMPHOBLASTIC-LEUKEMIA | EXPRESSION | Bone Marrow Cells - chemistry | Immunohistochemistry | Thrombocythemia, Essential - enzymology | Myeloproliferative Disorders - enzymology | Bone Marrow Cells - enzymology | United States | Humans | Leukemia, Myelomonocytic, Chronic - genetics | Polycythemia Vera - blood | Leukemia, Myelogenous, Chronic, BCR-ABL Positive - genetics | Hematopoiesis, Extramedullary - genetics | Polycythemia Vera - genetics | Myelodysplastic Syndromes - blood | Thrombocythemia, Essential - genetics | Myeloproliferative Disorders - genetics | Megakaryocytes - chemistry | Myelodysplastic Syndromes - enzymology | Primary Myelofibrosis - blood | Myeloproliferative Disorders - blood | Leukemia, Myeloid, Acute - enzymology | Spleen - enzymology | Lasers | Leukemia, Myelomonocytic, Chronic - enzymology | Janus Kinase 2 - metabolism | Myeloproliferative Disorders - metabolism | Leukemia, Myelomonocytic, Chronic - blood | Polymerase Chain Reaction | Retrospective Studies | Leukemia, Myelogenous, Chronic, BCR-ABL Positive - enzymology | Leukemia, Myelogenous, Chronic, BCR-ABL Positive - blood | Janus Kinase 2 - genetics | Polycythemia Vera - enzymology | Leukemia, Myeloid, Acute - blood | Thrombocythemia, Essential - blood | bcl-X Protein - analysis | Megakaryocytes - enzymology | Spleen - chemistry | Primary Myelofibrosis - enzymology | Microdissection - methods | Primary Myelofibrosis - genetics | Myelodysplastic Syndromes - genetics | Mutation | Chronic Disease | Leukemia, Myeloid, Acute - genetics
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11. Full Text Indoleamine 2,3-dioxygenase is a critical regulator of acute graft-versus-host disease lethality
by Jasperson, Lisa K and Bucher, Christoph and Panoskaltsis-Mortari, Angela and Taylor, Patricia A and Mellor, Andrew L and Munn, David H and Blazar, Bruce R
Blood, ISSN 0006-4971, 03/2008, Volume 111, Issue 6, pp. 3257 - 3265
Graft-versus-host disease (GVHD) is initiated after activation of donor T cells by host antigen-presenting cells (APCs). The immunosuppressive enzyme... 
INHIBITION | DENDRITIC CELLS | BONE-MARROW | SUBSETS | MICE | INDUCTION | HEMATOLOGY | EXPRESSION | T-CELLS | TRYPTOPHAN CATABOLISM | CUTTING EDGE | Colon - cytology | Indoleamine-Pyrrole 2,3,-Dioxygenase - genetics | Indoleamine-Pyrrole 2,3,-Dioxygenase - metabolism | Up-Regulation | Colon - enzymology | T-Lymphocytes - enzymology | Indoleamine-Pyrrole 2,3,-Dioxygenase - deficiency | Lymph Nodes - enzymology | Graft vs Host Disease - genetics | Spleen - enzymology | Sensitivity and Specificity | Acute Disease | Survival Rate | Spleen - cytology | Lymph Nodes - cytology | Graft vs Host Disease - pathology | Mice, Knockout | Phenotype | Animals | T-Lymphocytes - cytology | Genes, Lethal - genetics | Mice | Tissue Donors | Graft vs Host Disease - enzymology | Apoptosis | Transplantation
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12. Full Text Immunoprotection and Functional Improvement of Allogeneic Islets in Diabetic Mice, Using a Stable Indoleamine 2,3-Dioxygenase Producing Scaffold
by Hosseini-Tabatabaei, Azadeh and Jalili, Reza Baradar and Khosravi-Maharlooei, Mohsen and Hartwell, Ryan and Kilani, Ruhangiz T and Zhang, Yun and Ghahary, Aziz
Transplantation, ISSN 0041-1337, 07/2015, Volume 99, Issue 7, pp. 1341 - 1348
BACKGROUNDWe have previously shown that an immunomodulatory enzyme, indoleamine 2,3-dioxygenase (IDO) in dermal fibroblasts generates a tryptophan-deficient... 
SURVIVAL | SURGERY | PANCREATIC-ISLETS | THERAPY | 2,3 DIOXYGENASE | VIABILITY | MOUSE | IMMUNOLOGY | EXPRESSION | TRANSPLANTATION | STRATEGIES | Indoleamine-Pyrrole 2,3,-Dioxygenase - genetics | Fibroblasts - enzymology | Cell Proliferation | Fibroblasts - transplantation | Spleen - immunology | T-Lymphocytes - enzymology | Diabetes Mellitus, Experimental - enzymology | Coculture Techniques | Diabetes Mellitus, Experimental - genetics | Male | Islets of Langerhans - surgery | Diabetes Mellitus, Experimental - therapy | Diabetes Mellitus, Experimental - blood | Lymph Nodes - enzymology | Tissue Scaffolds | Transfection | Spleen - enzymology | Time Factors | Indoleamine-Pyrrole 2,3,-Dioxygenase - biosynthesis | Islets of Langerhans - enzymology | Lymphocyte Activation | Tissue Culture Techniques | Graft Rejection - prevention & control | Mice, Inbred C57BL | Cells, Cultured | Islets of Langerhans - immunology | Graft Survival | Biomarkers - blood | Islets of Langerhans Transplantation - methods | Lymph Nodes - immunology | Diabetes Mellitus, Experimental - immunology | Animals | Fibroblasts - immunology | T-Lymphocytes - immunology | Mice, Inbred BALB C | Graft Rejection - immunology | Blood Glucose - metabolism | Genetic Therapy - methods
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13. Full Text Localization and Differential Expression of Activation-Induced Cytidine Deaminase in the Amphibian Xenopus upon Antigen Stimulation and during Early Development
by Marr, Shauna and Morales, Heidi and Bottaro, Andrea and Cooper, Michelle and Flajnik, Martin and Robert, Jacques
The Journal of Immunology, ISSN 0022-1767, 11/2007, Volume 179, Issue 10, pp. 6783 - 6789
As in mammals, B cell maturation in the amphibian Xenopus involves somatic hypermutation (SHM) and class switch recombination to diversify the B cell receptor... 
SYSTEM | CENTER B-CELLS | IMMUNE-RESPONSE | LAEVIS | FROG XENOPUS | AID GENE | VERTEBRATES | CLASS-SWITCH RECOMBINATION | IMMUNOGLOBULIN CLASS | IMMUNOLOGY | FAMILY | Bacterial Infections - enzymology | Cytidine Deaminase - immunology | Spleen - embryology | Liver - enzymology | Somatic Hypermutation, Immunoglobulin - immunology | Spleen - immunology | Germinal Center - immunology | Antigens, Bacterial - immunology | Germinal Center - enzymology | Immunoglobulin Class Switching - immunology | Liver - embryology | Gene Expression Regulation, Developmental - immunology | Cytidine Deaminase - biosynthesis | Liver - immunology | Larva - immunology | Spleen - enzymology | Bacterial Infections - immunology | Larva - growth & development | Xenopus Proteins - biosynthesis | Larva - enzymology | Recombination, Genetic - immunology | B-Lymphocytes - enzymology | Virus Diseases - immunology | Xenopus Proteins - immunology | Xenopus laevis | Mammals | Receptors, Antigen, B-Cell - immunology | Biological Evolution | Antigens, Viral - immunology | Cell Differentiation - immunology | Virus Diseases - enzymology | Animals | B-Lymphocytes - immunology | Up-Regulation - immunology | Enzyme Activation | Gene Expression Regulation, Enzymologic - immunology
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14. Full Text Myeloperoxidase: A Leukocyte-Derived Protagonist of Inflammation and Cardiovascular Disease
by Nussbaum, Claudia and Klinke, Anna and Adam, Matti and Baldus, Stephan and Sperandio, Markus
Antioxidants & Redox Signaling, ISSN 1523-0864, 02/2013, Volume 18, Issue 6, pp. 692 - 713
Significance: The heme-enzyme myeloperoxidase (MPO) is one of the major neutrophil bactericidal proteins and is stored in large amounts inside azurophilic... 
Forum Review Articles | CHRONIC HEART-FAILURE | NEUTROPHIL EXTRACELLULAR TRAPS | HUMAN ATHEROSCLEROTIC INTIMA | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENDOCRINOLOGY & METABOLISM | LOW-DENSITY-LIPOPROTEIN | SPLEEN GREEN HEMEPROTEIN | ACUTE CORONARY SYNDROMES | INNATE IMMUNE-SYSTEM | ELEVATION MYOCARDIAL-INFARCTION | OXIDANT HYPOCHLOROUS ACID | RAY CRYSTAL-STRUCTURE | Inflammation - pathology | Cardiovascular Diseases - metabolism | Humans | Infection - enzymology | Infection - microbiology | Cardiovascular Diseases - enzymology | Cardiovascular Diseases - pathology | Leukocytes - enzymology | Inflammation - metabolism | Infection - pathology | Leukocytes - microbiology | Neutrophils - microbiology | Inflammation - enzymology | Neutrophils - metabolism | Hypochlorous Acid - metabolism | Peroxidase - metabolism | Physiological aspects | Peroxidase | Inflammation | Cardiovascular diseases | Analysis
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