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المؤلفون: Vincent Olieric, Warispreet Singh, Irina G. Tikhonova, Dietmar Weichert, Eoin M. Scanlan, Martin Caffrey, Chia-Ying Huang, Katherine Bowen, Samir Olatunji
المصدر: Nature Communications
Olatunji, S, Bowen, K, Huang, C-Y, Weichert, D, Singh, W, Tikhonova, I G, Scanlan, E M, Olieric, V & Caffrey, M 2021, ' Structural basis of the membrane intramolecular transacylase reaction responsible for lyso-form lipoprotein synthesis ', Nature Communications, vol. 12, 4254 . https://doi.org/10.1038/s41467-021-24475-0Test
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)مصطلحات موضوعية: Bacterial immune evasion, Stereochemistry, Science, Acylation, Lipoproteins, DNA Mutational Analysis, General Physics and Astronomy, Article, General Biochemistry, Genetics and Molecular Biology, Bacterial cell structure, Substrate Specificity, Structure-Activity Relationship, 03 medical and health sciences, 0302 clinical medicine, Transacylation, Bacterial Proteins, Catalytic Domain, Moiety, Amino Acid Sequence, Cysteine, Conserved Sequence, X-ray crystallography, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Multidisciplinary, Cell Membrane, C100, General Chemistry, C700, C900, Transmembrane domain, Enzyme, chemistry, Enzyme mechanisms, Protein Processing, Post-Translational, Acyltransferases, 030217 neurology & neurosurgery, Function (biology), Lipoprotein
وصف الملف: application/pdf
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::196eb1c8b674739869ff2bbe30bcb495Test
https://nrl.northumbria.ac.uk/id/eprint/46670/1/41467_2021_Article_24475.pdfTest -
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المؤلفون: Thomas S. Moody, Qi Wu, Manfred T. Reetz, Warispreet Singh, Jiahai Zhou, Yixin Cen, Mamatjan Arkin, Meilan Huang
المصدر: Nature Communications
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Cen, Y, Singh, W, Arkin, M, Moody, T S, Huang, M, Zhou, J, Wu, Q & Reetz, M T 2019, ' Artificial cysteine-lipases with high activity and altered catalytic mechanism created by laboratory evolution ', Nature Communications, vol. 10, 3198 . https://doi.org/10.1038/s41467-019-11155-3Testمصطلحات موضوعية: 0301 basic medicine, Models, Molecular, Stereochemistry, Protein Conformation, Science, Protein design, General Physics and Astronomy, 02 engineering and technology, Crystallography, X-Ray, Protein Engineering, General Biochemistry, Genetics and Molecular Biology, Catalysis, Article, Substrate Specificity, Fungal Proteins, 03 medical and health sciences, Enzyme activator, Catalytic Domain, Hydrolase, Catalytic triad, Cysteine, Lipase, lcsh:Science, Candida, chemistry.chemical_classification, Multidisciplinary, Binding Sites, biology, Hydrolysis, General Chemistry, 021001 nanoscience & nanotechnology, Directed evolution, biology.organism_classification, C700, Enzyme Activation, Kinetics, 030104 developmental biology, Enzyme, chemistry, Mutation, Enzyme mechanisms, biology.protein, Biocatalysis, lcsh:Q, Candida antarctica, 0210 nano-technology
وصف الملف: application/pdf
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d2bb96f00aa229bf6570d77d01eedabTest
https://nrl.northumbria.ac.uk/id/eprint/43298/1/s41467-019-11155-3.pdfTest -
3دورية أكاديمية
المؤلفون: Ballandras-Colas, Allison, Brown, Monica, Cook, Nicola J., Dewdney, Tamaria G., Demeler, Borries, Cherepanov, Peter, Lyumkis, Dmitry, Engelman, Alan N.
مصطلحات موضوعية: Cryoelectron microscopy, DNA recombination, Enzyme mechanisms, Retrovirus, Betaretroviruses, Retroviruses
وصف الملف: application/pdf
العلاقة: Ballandras-Colas, A., Brown, M., Cook, N. J., Dewdney, T. G., Demeler, B., Cherepanov, P., Lyumkis, D., & Engelman, A. N. (2016). Cryo-EM reveals a novel octameric integrase structure for betaretroviral intasome function. Nature, 530, 358-361. https://doi.org/10.1038/nature16955Test; https://hdl.handle.net/10133/6067Test
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4دورية أكاديمية
المؤلفون: Bhattacharya, Akash, Wang, Zhonghua, White, Tommy, Buffone, Cindy, Nguyen, Laura A., Shepard, Caitlin N., Kim, Baek, Demeler, Borries, Diaz-Griffero, Felipe, Ivanov, Dmitri N.
مصطلحات موضوعية: Enzyme mechanisms, Phosphomimetic mutations, SAMHD1, Tetramer stability, Retroviral, HIV infections
وصف الملف: application/pdf
العلاقة: Bhattacharya, A., Wang, Z., White, T., Buffone, C., Nguyen, L. A., Shepard, C. N., Kim, B., Demeler, B., Diaz-Griffero, F., & Ivanov, D. N. (2016). Effects of T592 phosphomimetric mutations on tetramer stability and dNTPase activity of SAMHD1 can not explain the retroviral restriction defect. Scientific Reports, 6, Article 31353. https://doi.org/10.1038/srep31353Test; https://hdl.handle.net/10133/6058Test
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5مورد إلكتروني
مصطلحات الفهرس: Enzyme mechanisms, Phosphomimetic mutations, SAMHD1, Tetramer stability, Retroviral, Article
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8مورد إلكتروني
مصطلحات الفهرس: Enzyme mechanisms, Phosphomimetic mutations, SAMHD1, Tetramer stability, Retroviral, Article
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10مورد إلكتروني
مصطلحات الفهرس: Enzyme mechanisms, Phosphomimetic mutations, SAMHD1, Tetramer stability, Retroviral, Article