G. Louie

发表

Molecular recognition in protein families: a database of aligned three-dimensional structures of related proteins.

John P. Overington, A. Sali, Z. Y. Zhu, 1993, Biochemical Society transactions.

Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site

T. Blundell, J. Cooper, G. Louie, 1992, Nature.

Architectures, mechanisms and molecular evolution of natural product methyltransferases.

J. Noel, G. Louie, D. Liscombe, 2012, Natural product reports.

Structural analysis of a set of proteins resulting from a bacterial genomics project

B. Laubert, J. M. Sauder, K. Gajiwala, 2005, Proteins.

Evolution of the Chalcone Isomerase Fold from Fatty Acid-Binding to Stereospecific Enzyme

Eve Syrkin Wurtele, Gerard Manning, M. Bowman, 2012, Nature.

Energetic components of the allosteric machinery in hemoglobin measured by hydrogen exchange.

S W Englander, G. Louie, S. Englander, 1998, Journal of molecular biology.

Purification, characterization, crystallisation and X-ray analysis of selenomethionine-labelled hydroxymethylbilane synthase from Escherichia coli.

V. Malashkevich, G. Louie, C. Abell, 1993, European journal of biochemistry.

Genetically encoding photoswitchable click amino acids in Escherichia coli and mammalian cells.

Joseph P Noel, J. Noel, G. Louie, 2014, Angewandte Chemie.

Bifunctional Substrate Activation via an Arginine Residue Drives Catalysis in Chalcone Isomerases

Dan S. Tawfik, M. Bowman, J. Noel, 2018, bioRxiv.

Role of phenylalanine-82 in yeast iso-1-cytochrome c and remote conformational changes induced by a serine residue at this position.

G J Pielak, G. Brayer, G. Louie, 1988, Biochemistry.

The three‐dimensional structures of mutants of porphobilinogen deaminase: Toward an understanding of the structural basis of acute intermittent porphyria

T. Blundell, J. Cooper, G. Louie, 1994, Protein science : a publication of the Protein Society.

Crystallization and preliminary X-ray investigation of Escherichia coli porphobilinogen deaminase.

T. Blundell, J. Cooper, G. Louie, 1992, Journal of molecular biology.

Modulation of auxin formation by the cytosolic phenylalanine biosynthetic pathway

I. Maoz, M. Bowman, J. Noel, 2020, Nature Chemical Biology.

Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases.

M. Bowman, B. Moore, J. Noel, 2006, Chemistry & biology.

Discovery of two cyanobacterial phenylalanine ammonia lyases: kinetic and structural characterization.

M. Bowman, B. Moore, J. Noel, 2007, Biochemistry.

Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement

B. Moore, J. Noel, G. Louie, 2013, Nature.

High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c.

G. Brayer, G. Louie, G D Brayer, 1990, Journal of molecular biology.

Structure-Function Analyses of a Caffeic Acid O-Methyltransferase from Perennial Ryegrass Reveal the Molecular Basis for Substrate Preference[W][OA]

M. Bowman, J. Noel, G. Spangenberg, 2010, Plant Cell.

High-resolution three-dimensional structure of horse heart cytochrome c.

G. Brayer, G. Louie, G D Brayer, 1990, Journal of molecular biology.

Biosynthesis of coral settlement cue tetrabromopyrrole in marine bacteria by a uniquely adapted brominase–thioesterase enzyme pair

M. Schorn, B. Moore, J. Noel, 2016, Proceedings of the National Academy of Sciences.

Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor.

M. Bowman, G. Louie, S. Choe, 1997, Molecular cell.

The multiple phenylpropene synthases in both Clarkia breweri and Petunia hybrida represent two distinct protein lineages.

M. Bowman, J. Noel, E. Pichersky, 2008, The Plant journal : for cell and molecular biology.

Functional Analyses of Caffeic Acid O-Methyltransferase and Cinnamoyl-CoA-Reductase Genes from Perennial Ryegrass (Lolium perenne)[W]

German Spangenberg, Pieter Badenhorst, Zhiqian Liu, 2010, Plant Cell.

Yeast iso-1-cytochrome c. A 2.8 A resolution three-dimensional structure determination.

G. Brayer, G. Louie, W. Hutcheon, 1988, Journal of molecular biology.

Genetically Encoding Unnatural Amino Acids in Neural Stem Cells and Optically Reporting Voltage‐Sensitive Domain Changes in Differentiated Neurons

Barbara Miller, Lei Wang, Joseph P Noel, 2011, Stem cells.

Characterization of human blood coagulation factor XII cDNA. Prediction of the primary structure of factor XII and the tertiary structure of beta-factor XIIa.

R T MacGillivray, G. Brayer, G. Louie, 1985, The Journal of biological chemistry.

Porphobilinogen deaminase and its structural similarity to the bidomain binding proteins

G. Louie, 1993 .

Detection of a high mutation frequency in exon 12 of the porphobilinogen deaminase gene in patients with acute intermittent porphyria

G. Louie, W. Lanyon, J. Connor, 1993, Human Genetics.

Tight binding affinities determined from thermodynamic linkage to protons by titration calorimetry.

M. Doyle, G. Louie, T. Sokoloski, 1995, Methods in enzymology.

Substrate specificity and engineering of mevalonate 5-phosphate decarboxylase.

J. Noel, G. Louie, V. Lundblad, 2019, ACS chemical biology.

Structural Studies of Cinnamoyl-CoA Reductase and Cinnamyl-Alcohol Dehydrogenase, Key Enzymes of Monolignol Biosynthesis[C][W]

R. Dixon, M. Bowman, J. Noel, 2014, Plant Cell.

A polypeptide chain-refolding event occurs in the Gly82 variant of yeast iso-1-cytochrome c.

G. Brayer, G. Louie, Gordon V. Louie, 1989, Journal of molecular biology.

Allosteric energy at the hemoglobin beta chain C terminus studied by hydrogen exchange.

G. Louie, S. Englander, J. J. Englander, 1988, Journal of molecular biology.

Genetically encoding unnatural amino acids for cellular and neuronal studies

J. Noel, G. Louie, P. Slesinger, 2007, Nature Neuroscience.

The three‐dimensional structure of Escherichia coli porphobilinogen deaminase at 1.76‐Å resolution

T. Blundell, J. Cooper, G. Louie, 1996, Proteins: Structure, Function, and Bioinformatics.

Salt, phosphate and the Bohr effect at the hemoglobin beta chain C terminus studied by hydrogen exchange.

G. Louie, S. Englander, J. J. Englander, 1988, Journal of molecular biology.

Biosynthetic potential of sesquiterpene synthases: product profiles of Egyptian Henbane premnaspirodiene synthase and related mutants

M. Bowman, J. Noel, G. Louie, 2016, The Journal of Antibiotics.

Structural studies of the roles of residues 82 and 85 at the interactive face of cytochrome c.

G. Brayer, G. Louie, M. Smith, 1994, Biochemistry.

Structure and Reaction Mechanism of Basil Eugenol Synthase

M. Bowman, J. Noel, E. Pichersky, 2007, PloS one.

Expanding the Library and Substrate Diversity of the Pyrrolysyl‐tRNA Synthetase to Incorporate Unnatural Amino Acids Containing Conjugated Rings

J. Noel, G. Louie, Vanessa K. Lacey, 2013, Chembiochem : a European journal of chemical biology.

Structural studies on porphobilinogen deaminase.

T. Blundell, G. Louie, S. Wood, 1994, Ciba Foundation symposium.

Identification of five novel mutations in the porphobilinogen deaminase gene.

G. Louie, W. Lanyon, J. Connor, 1994, Human Molecular Genetics.

Structure of the pseudouridine synthase RsuA from Haemophilus influenzae.

S. Burley, G. Louie, A. Matte, 2005, Acta crystallographica. Section F, Structural biology and crystallization communications.

Carson Motivates Minorities

M. Bowman, E. Pichersky, G. Louie, 1995, Environmental Health Perspectives.

Biochemistry and Protein Interactions of the CYREN Microprotein.

M. Bowman, G. Louie, Maziar S. Ardejani, 2023, Biochemistry.

Visualizing the Interface of Biotin and Fatty Acid Biosynthesis through SuFEx Probes.

M. Bowman, G. Louie, J. L. La Clair, 2024, Journal of the American Chemical Society.

A moderate form of hemophilia B is caused by a novel mutation in the protease domain of factor IXVancouver.

R. MacGillivray, G. Brayer, G. Louie, 1989, The Journal of biological chemistry.