نتائج البحث - "Wyatt W, Yue"

1

Defining substrate selection by rhinoviral 2A proteinase through its crystal structure with the inhibitor zVAM.fmk

المؤلفون: Gustavo Arruda Bezerra, Tim Skern, Wyatt W. Yue, Karin M. Deutschmann-Olek

المصدر: Virology. 562:128-141

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::383529bffe662fb2773cde3ad54d9453Test
https://doi.org/10.1016/j.virol.2021.07.008Test

2

Succinyl-CoA:3-oxoacid coenzyme A transferase (SCOT) deficiency: A rare and potentially fatal metabolic disease

المؤلفون: Wyatt W. Yue, Sabrina Mackinnon, Melanie Walter, Raina Yamamoto, William Foster, Sylvia Roloff, Anke Schumann, Sarah C. Grünert, Lisa Stübbe, Ali Alasmari, Ute Spiekerkoetter, Osama A. Obaid, Eissa Faqeih, Allan M. Lund, Christina Pontes, Corinne Gemperle-Britschgi, Jörn Oliver Sass, Natalie Weinhold

المصدر: Biochimie. 183:55-62

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf49788580b3d54a2a07377626afd22fTest
https://doi.org/10.1016/j.biochi.2021.02.003Test

3

Fragment Screening Reveals Starting Points for Rational Design of Galactokinase 1 Inhibitors to Treat Classic Galactosemia

المؤلفون: W. Foster, G Arruda Bezerra, T. Krojer, Manshu Tang, Huber Kvm., Kent Lai, L. Diaz-Saez, Sabrina Mackinnon, Wyatt W. Yue, F. von Delft, Paul Brennan

المصدر: ACS Chemical Biology

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c6526484f4e04cc09ef4d380ce28a82Test
https://doi.org/10.1021/acschembio.0c00498Test

4

Molecular basis for the regulation of human glycogen synthase by phosphorylation and glucose-6-phosphate

المؤلفون: I. M. Ferreira, Wyatt W. Yue, D. S. Froese, L. Shrestha, T. J. McCorvie, M. Tu, Seungil Han, Paula M. Loria, A. P. Berg

مصطلحات موضوعية: Conformational change, chemistry.chemical_compound, Glycogenin, Glucose 6-phosphate, chemistry, Biochemistry, Glycogen, biology, Phosphatase, Allosteric regulation, biology.protein, Phosphorylation, Glycogen synthase

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_________::59da5a15b680c88b18b55d4f27839ec4Test
https://doi.org/10.1101/2021.11.12.468446Test

5

Structure of the human frataxin-bound iron-sulfur cluster assembly complex provides insight into its activation mechanism

المؤلفون: Alain Martelli, Claire Strain-Damerell, Henry J. Bailey, Christine Bulawa, Xiaodi Yu, Seungil Han, Wyatt W. Yue, Nicholas G. Fox, Joseph F. Nabhan, Xidong Feng

المصدر: Nature Communications, Vol 10, Iss 1, Pp 1-8 (2019)
Nature Communications

مصطلحات موضوعية: Iron-Sulfur Proteins, Models, Molecular, Scaffold protein, inorganic chemicals, Iron, Science, 010402 general chemistry, 01 natural sciences, Iron-sulfur cluster assembly complex, digestive system, Article, 03 medical and health sciences, chemistry.chemical_compound, Biosynthesis, Iron-Binding Proteins, lcsh:Science, 030304 developmental biology, 0303 health sciences, biology, Cysteine desulfurase, Activator (genetics), Cryoelectron Microscopy, fungi, SAXS, Recombinant Proteins, Mitochondria, 0104 chemical sciences, 3. Good health, Cell biology, Carbon-Sulfur Lyases, Zinc, chemistry, Friedreich Ataxia, Mitochondrial matrix, Enzyme mechanisms, Frataxin, biology.protein, lcsh:Q, ISCU, Sulfur

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53ea331aa8af6309e6f2c081bd2451e1Test
https://doaj.org/article/8abcf6459af9457bb7545657bbc6ed8dTest

6

4′-Phosphopantetheine and long acyl chain-dependent interactions are integral to human mitochondrial acyl carrier protein function

المؤلفون: Wyatt W. Yue, Alain Martelli, Theresa Towle, Christine Bulawa, Joseph F. Nabhan, Renea Gooch, Xidong Feng, Tiffany Ma, Nicholas G. Fox, Jaimeen D. Majmudar

المصدر: MedChemComm. 10:209-220

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a55720aed23cd65b2fdf1a60e5461cfTest
https://doi.org/10.1039/c8md00489gTest

7

Identification of small molecule allosteric modulators of 5,10-methylenetetrahydrofolate reductase (MTHFR) by targeting its unique regulatory domain

المؤلفون: Alexander Holenstein, W. Foster, Arindam Talukdar, D. Sean Froese, Bing Xie, Wyatt W. Yue, Gustavo Arruda Bezerra, Céline Bürer, Debomita Bhattacharya, Lei Shi, Seraina Lutz, Ayan Mukherjee, Kevin G. Hicks, Jared Rutter, Peter Brown, Minkui Luo, Dipika Sarkar

المساهمون: University of Zurich, Froese, D Sean, Yue, Wyatt W

المصدر: Biochimie

مصطلحات موضوعية: 0301 basic medicine, S-Adenosylmethionine, 1303 Biochemistry, Methylenetetrahydrofolate reductase deficiency, 5,10-Methylenetetrahydrofolate reductase, Drug-development, Allosteric regulation, 610 Medicine & health, Reductase, Biochemistry, Article, 03 medical and health sciences, chemistry.chemical_compound, Sinefungin, Allosteric Regulation, Protein Domains, Enzymatic inhibition, medicine, Humans, Enzyme Inhibitors, Methylenetetrahydrofolate Reductase (NADPH2), Methionine, 030102 biochemistry & molecular biology, biology, Small molecules, General Medicine, medicine.disease, Small molecule, digestive system diseases, One-carbon metabolism, 030104 developmental biology, chemistry, 10036 Medical Clinic, Docking (molecular), Methylenetetrahydrofolate reductase, biology.protein

وصف الملف: 1_s2.0_S0300908421000092_main.pdf - application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef61fcca8498f1f66e36e94dcc833f49Test

8

Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release

المؤلفون: Gopalakrishnan Bulusu, Robert J. Desnick, David F. Bishop, W. Foster, Siladitya Padhi, Arijit Roy, Wyatt W. Yue, Elzbieta Rembeza, Harry A. Dailey, Jason R. Marcero, Gustavo Arruda Bezerra, Henry J. Bailey

المصدر: Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
Nature Communications

مصطلحات موضوعية: 0301 basic medicine, Protoporphyria, Erythropoietic, Protein Conformation, Science, Protein domain, General Physics and Astronomy, Heme, Plasma protein binding, Molecular Dynamics Simulation, Crystallography, X-Ray, Isozyme, Catalysis, Gene Expression Regulation, Enzymologic, Article, General Biochemistry, Genetics and Molecular Biology, Substrate Specificity, Frameshift mutation, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Protein structure, Protein Domains, Transferases, Catalytic Domain, Humans, lcsh:Science, X-ray crystallography, Multidisciplinary, biology, Chemistry, Active site, Genetic Diseases, X-Linked, General Chemistry, ALAS2, Kinetics, 030104 developmental biology, Enzyme mechanisms, biology.protein, Biophysics, lcsh:Q, Acyl Coenzyme A, 030217 neurology & neurosurgery, 5-Aminolevulinate Synthetase, Protein Binding

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::285537360df796d460f3e2ba3ac1a931Test
https://doi.org/10.1038/s41467-020-16586-xTest

9

Naturally occurring cobalamin (B12) analogs can function as cofactors for human methylmalonyl-CoA mutase

المؤلفون: Michiko E. Taga, Sabrina Mackinnon, D. Sean Froese, Olga M. Sokolovskaya, Henry J. Bailey, Wyatt W. Yue, Tanja Plessl, Matthias R. Baumgartner

المساهمون: University of Zurich, Taga, Michiko E

مصطلحات موضوعية: 0301 basic medicine, Biochemistry & Molecular Biology, 1303 Biochemistry, Vitamin B-12, 1.1 Normal biological development and functioning, Coenzymes, 610 Medicine & health, Context (language use), Cobamide, Biochemistry, Cobalamin, Cofactor, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Mutase, Underpinning research, polycyclic compounds, Humans, Vitamin B12, Vitamin B(12), 030304 developmental biology, Nutrition, chemistry.chemical_classification, 0303 health sciences, Methylmalonic aciduria, 030102 biochemistry & molecular biology, biology, Chemistry, Methylmalonyl-CoA mutase, nutritional and metabolic diseases, Methylmalonyl-CoA Mutase, General Medicine, 3. Good health, Vitamin B 12, Kinetics, 030104 developmental biology, Enzyme, 10036 Medical Clinic, biology.protein, Biochemistry and Cell Biology, 030217 neurology & neurosurgery, Function (biology), MMUT

وصف الملف: application/pdf; nihms_1618799.pdf - application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5f2d8b2c6a727b4a2f45830438cf4a5Test

10

Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition

المؤلفون: Elzbieta Rembeza, D. Sean Froese, Terttu Suormala, Anselm Erich Oberholzer, Oktawia Borkowska, Wyatt W. Yue, Jolanta Kopec, Gustavo Arruda Bezerra, Rod Chalk, Seraina Lutz, Matthias R. Baumgartner

المساهمون: University of Zurich, Froese, D Sean

المصدر: Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
Nature Communications

مصطلحات موضوعية: 0301 basic medicine, Models, Molecular, Protein Folding, S-Adenosylmethionine, General Physics and Astronomy, Reductase, Crystallography, X-Ray, Mass Spectrometry, chemistry.chemical_compound, 0302 clinical medicine, Protein structure, X-Ray Diffraction, Catalytic Domain, Phosphorylation, lcsh:Science, Multidisciplinary, biology, Chemistry, 3100 General Physics and Astronomy, Recombinant Proteins, Biochemistry, Science, Protein domain, Allosteric regulation, 610 Medicine & health, 1600 General Chemistry, Molecular Dynamics Simulation, General Biochemistry, Genetics and Molecular Biology, Article, Evolution, Molecular, 03 medical and health sciences, Biosynthesis, Protein Domains, 1300 General Biochemistry, Genetics and Molecular Biology, Scattering, Small Angle, Humans, Amino Acid Sequence, Protein Structure, Quaternary, Methylenetetrahydrofolate Reductase (NADPH2), Methionine, General Chemistry, digestive system diseases, Kinetics, 030104 developmental biology, 10036 Medical Clinic, Methylenetetrahydrofolate reductase, biology.protein, lcsh:Q, 030217 neurology & neurosurgery, NADP

وصف الملف: 41467_2018_Article_4735.pdf - application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25c668c6b07c00337b17f534542d0bceTest
http://link.springer.com/article/10.1038/s41467-018-04735-2Test

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