A microbial sulfoquinovose monooxygenase pathway enables sulfosugar assimilation
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Nichollas E. Scott | Spencer J. Williams | G. Davies | E. Saunders | M. McConville | D. Ascher | E. Goddard-Borger | Mahima Sharma | J. Lingford | M. Petricevic | Yunyang Zhang | R. Epa | A. Snow | M. Jarva | Runyao Mao | Janice Mui | B. D. da Silva | D. Pires
[1] D. Dowling,et al. Structures of the alkanesulfonate monooxygenase MsuD provide insight into C–S bond cleavage, substrate scope, and an unexpected role for the tetramer , 2021, The Journal of biological chemistry.
[2] Cameron L.M. Gilchrist,et al. clinker & clustermap.js: Automatic generation of gene cluster comparison figures , 2020, bioRxiv.
[3] Huimin Zhao,et al. A transaldolase-dependent sulfoglycolysis pathway in Bacillus megaterium DSM 1804. , 2020, Biochemical and biophysical research communications.
[4] Spencer J. Williams,et al. The Molecular Basis of Sulfosugar Selectivity in Sulfoglycolysis , 2020 .
[5] O. Acevedo,et al. Substrate-Dependent Mobile Loop Conformational Changes in Alkanesulfonate Monooxygenase from Accelerated Molecular Dynamics. , 2020, Biochemistry.
[6] Alexander Loy,et al. Environmental and Intestinal Phylum Firmicutes Bacteria Metabolize the Plant Sugar Sulfoquinovose via a 6-Deoxy-6-sulfofructose Transaldolase Pathway , 2020, iScience.
[7] Nichollas E. Scott,et al. A Sulfoglycolytic Entner-Doudoroff Pathway in Rhizobium leguminosarum bv. trifolii SRDI565 , 2019, Applied and Environmental Microbiology.
[8] Spencer J. Williams,et al. Dynamic Structural Changes Accompany the Production of Dihydroxypropanesulfonate by Sulfolactaldehyde Reductase , 2019, ACS Catalysis.
[9] P. Bork,et al. Interactive Tree Of Life (iTOL) v4: recent updates and new developments , 2019, Nucleic Acids Res..
[10] Spencer J. Williams,et al. Comprehensive Synthesis of Substrates, Intermediates, and Products of the Sulfoglycolytic Embden-Meyerhoff-Parnas Pathway. , 2019, The Journal of organic chemistry.
[11] Martin Eisenacher,et al. The PRIDE database and related tools and resources in 2019: improving support for quantification data , 2018, Nucleic Acids Res..
[12] P. Agarwal,et al. Differential Substrate Recognition by Maltose Binding Proteins Influenced by Structure and Dynamics. , 2018, Biochemistry.
[13] Michael J. Dagley,et al. DExSI: a new tool for the rapid quantitation of 13C-labelled metabolites detected by GC-MS , 2018, Bioinform..
[14] Spencer J. Williams,et al. Sulfoquinovose in the biosphere: occurrence, metabolism and functions. , 2017, The Biochemical journal.
[15] Saulius Gražulis,et al. AceDRG: a stereochemical description generator for ligands , 2017, Acta crystallographica. Section D, Structural biology.
[16] Juan Antonio Vizcaíno,et al. The ProteomeXchange consortium in 2017: supporting the cultural change in proteomics public data deposition , 2016, Nucleic Acids Res..
[17] Spencer J. Williams,et al. YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids. , 2016, Nature chemical biology.
[18] D. Spiteller,et al. Entner–Doudoroff pathway for sulfoquinovose degradation in Pseudomonas putida SQ1 , 2015, Proceedings of the National Academy of Sciences.
[19] T. Penning,et al. The aldo-keto reductases (AKRs): Overview. , 2015, Chemico-biological interactions.
[20] Matthias Mann,et al. Visualization of LC‐MS/MS proteomics data in MaxQuant , 2015, Proteomics.
[21] Marco Y. Hein,et al. Accurate Proteome-wide Label-free Quantification by Delayed Normalization and Maximal Peptide Ratio Extraction, Termed MaxLFQ * , 2014, Molecular & Cellular Proteomics.
[22] Michael Weiss,et al. Sulphoglycolysis in Escherichia coli K-12 closes a gap in the biogeochemical sulphur cycle , 2014, Nature.
[23] Pelin Yilmaz,et al. The SILVA and “All-species Living Tree Project (LTP)” taxonomic frameworks , 2013, Nucleic Acids Res..
[24] M. Udvardi,et al. Transport and metabolism in legume-rhizobia symbioses. , 2013, Annual review of plant biology.
[25] R. Breitling,et al. Detecting Sequence Homology at the Gene Cluster Level with MultiGeneBlast , 2013, Molecular biology and evolution.
[26] M. Sagi,et al. The determination of sulfite levels and its oxidation in plant leaves. , 2012, Plant science : an international journal of experimental plant biology.
[27] Thomas Huhn,et al. Sulfoquinovose degraded by pure cultures of bacteria with release of C3-organosulfonates: complete degradation in two-member communities. , 2012, FEMS microbiology letters.
[28] S. McNicholas,et al. Presenting your structures: the CCP4mg molecular-graphics software , 2011, Acta crystallographica. Section D, Biological crystallography.
[29] Gregory Stephanopoulos,et al. Measuring deuterium enrichment of glucose hydrogen atoms by gas chromatography/mass spectrometry. , 2011, Analytical chemistry.
[30] Liisa Holm,et al. Dali server: conservation mapping in 3D , 2010, Nucleic Acids Res..
[31] Graeme Winter,et al. xia2: an expert system for macromolecular crystallography data reduction , 2010 .
[32] Randy J. Read,et al. Acta Crystallographica Section D Biological , 2003 .
[33] M. Mann,et al. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification , 2008, Nature Biotechnology.
[34] A. Wilkinson,et al. Higher-throughput approaches to crystallization and crystal structure determination. , 2008, Biochemical Society transactions.
[35] Jue Chen,et al. Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems , 2008, Microbiology and Molecular Biology Reviews.
[36] Z. Rao,et al. Crystal structure of long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN: unveiling the long-chain alkane hydroxylase. , 2008, Journal of molecular biology.
[37] K Henrick,et al. Electronic Reprint Biological Crystallography Secondary-structure Matching (ssm), a New Tool for Fast Protein Structure Alignment in Three Dimensions Biological Crystallography Secondary-structure Matching (ssm), a New Tool for Fast Protein Structure Alignment in Three Dimensions , 2022 .
[38] Kevin Cowtan,et al. research papers Acta Crystallographica Section D Biological , 2005 .
[39] Randy J Read,et al. Electronic Reprint Biological Crystallography Likelihood-enhanced Fast Rotation Functions Biological Crystallography Likelihood-enhanced Fast Rotation Functions , 2003 .
[40] M. Hewlins,et al. Glycolytic Breakdown of Sulfoquinovose in Bacteria: a Missing Link in the Sulfur Cycle , 2003, Applied and Environmental Microbiology.
[41] T. Richmond,et al. Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD. , 2002, Journal of molecular biology.
[42] 서정헌,et al. 반도체 공정 overview , 2001 .
[43] M. Kertesz. Riding the sulfur cycle--metabolism of sulfonates and sulfate esters in gram-negative bacteria. , 2000, FEMS microbiology reviews.
[44] T. Leisinger,et al. The Escherichia coli ssuEADCB Gene Cluster Is Required for the Utilization of Sulfur from Aliphatic Sulfonates and Is Regulated by the Transcriptional Activator Cbl* , 1999, The Journal of Biological Chemistry.
[45] G. Murshudov,et al. Refinement of macromolecular structures by the maximum-likelihood method. , 1997, Acta crystallographica. Section D, Biological crystallography.
[46] 廷冕 李,et al. 応用 (Application) について , 1981 .
[47] J. Harwood,et al. The plant sulpholipid-- a major component of the sulphur cycle. , 1979, Biochemical Society transactions.
[48] M. Mann,et al. Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips , 2007, Nature Protocols.
[49] P. Evans,et al. Scaling and assessment of data quality. , 2006, Acta crystallographica. Section D, Biological crystallography.
[50] B. Sörbo. Sulfate: turbidimetric and nephelometric methods. , 1987, Methods in enzymology.