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1دورية أكاديمية
المؤلفون: Jacqueline L Naffin-Olivos, Maria Georgieva, Nathan Goldfarb, Ranjna Madan-Lala, Lauren Dong, Erica Bizzell, Ethan Valinetz, Gabriel S Brandt, Sarah Yu, Daniil E Shabashvili, Dagmar Ringe, Ben M Dunn, Gregory A Petsko, Jyothi Rengarajan
المصدر: PLoS Pathogens, Vol 10, Iss 5, p e1004132 (2014)
مصطلحات موضوعية: Immunologic diseases. Allergy, RC581-607, Biology (General), QH301-705.5
وصف الملف: electronic resource
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المؤلفون: Dagmar Ringe, Kyoung-Shim Kim, Deog-Joong Kim, Inhye Jeong, Min-Joon Han, Mi-Jin Sohn, Eun-Hye Lee, Jisook Moon, Chun-Hyung Kim, Gregory A. Petsko, Jacqueline L. Naffin-Olivos, Quoc Toan Nguyen, Kwang-Soo Kim, Sreekanth Rajan, Chang-Hwan Park, Joon Shin, Ho Sup Yoon, Yupeng Tu, Baek-Soo Han, Won-Gon Kim
المساهمون: School of Biological Sciences
المصدر: Proceedings of the National Academy of Sciences. 112:8756-8761
مصطلحات موضوعية: Agonist, Parkinson's disease, medicine.drug_class, Neurogenesis, NR4A2, Drug target, Pharmacology, Ligands, Neuroprotection, Dopamine, Nuclear Receptor Subfamily 4, Group A, Member 2, Animals, Medicine, Oxidopamine, Transrepression, Orphan receptor, Multidisciplinary, Behavior, Animal, business.industry, Amodiaquine, Chloroquine, Parkinson Disease, Biological Sciences, medicine.disease, Rats, Disease Models, Animal, Nurr1, Dyskinesia, Nuclear receptor, Parkinson’s disease, medicine.symptom, business, Neuroscience, medicine.drug
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9c250077757730e5c6a0aaf8888616b
https://doi.org/10.1073/pnas.1509742112 -
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المؤلفون: Richard J. Auchus, Jacqueline L. Naffin-Olivos
المصدر: Biochemistry. 45:755-762
مصطلحات موضوعية: Models, Molecular, Mutation, Binding Sites, Cytochrome, biology, Allosteric regulation, Glutamic Acid, Lyases, Steroid 17-alpha-Hydroxylase, Stimulation, Steroid biosynthesis, medicine.disease_cause, Biochemistry, Cell Line, Substrate Specificity, Structure-Activity Relationship, Cytochromes b5, Targeted Mutation, Cytochrome b5, biology.protein, medicine, Humans, Point Mutation, Lyase activity
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المؤلفون: Dagmar Ringe, Maria Georgieva, Gregory A. Petsko, Nathan E. Goldfarb, Daniil Shabashvili, Lauren Dong, Gabriel S. Brandt, Erica Bizzell, Sarah Yu, Ethan Valinetz, Ranjna Madan-Lala, Ben M. Dunn, Jyothi Rengarajan, Jacqueline L. Naffin-Olivos
المصدر: PLoS Pathogens, Vol 10, Iss 5, p e1004132 (2014)
PLoS Pathogensمصطلحات موضوعية: Hydrolases, medicine.medical_treatment, Mutant, Pathogenesis, Pathology and Laboratory Medicine, Biochemistry, Serine, Mice, Medicine and Health Sciences, lcsh:QH301-705.5, Cells, Cultured, biology, medicine.diagnostic_test, Serine Endopeptidases, Serine hydrolase, Enzymes, Bacterial Pathogens, 3. Good health, Cell biology, Medical Microbiology, Host-Pathogen Interactions, Research Article, Protein Binding, lcsh:Immunologic diseases. Allergy, Proteases, Proteolysis, Immunology, Microbiology, Bacterial Proteins, Virology, Genetics, medicine, Animals, Microbial Pathogens, Molecular Biology, Serine protease, Protease, Macrophages, Immunity, Wild type, Biology and Life Sciences, Proteins, Chaperonin 60, Mycobacterium tuberculosis, Macrophage Activation, Molecular biology, Chaperone Proteins, Mice, Inbred C57BL, lcsh:Biology (General), Enzymology, biology.protein, Parasitology, Protein Multimerization, Serine Proteases, lcsh:RC581-607