F. Quiocho

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Human fatty acid synthase: structure and substrate selectivity of the thioesterase domain.

B. Chakravarty, Ziwei Gu, S. Chirala, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis.

F. Quiocho, A. Sharff, L. Rodseth, 1992, Biochemistry.

The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis.

F. Quiocho, J. Spurlino, G. Lu, 1992, The Journal of biological chemistry.

The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis.

F. Quiocho, J. Spurlino, G. Lu, 1992 .

Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein.

M. N. Vyas, F. Quiocho, N. Vyas, 1988, Science.

Architecture of the herpes simplex virus major capsid protein derived from structural bioinformatics.

F. Quiocho, M. Baker, W. Chiu, 2003, Journal of molecular biology.

Structure of the herpesvirus major capsid protein

F. Quiocho, M. Baker, W. Chiu, 2003, The EMBO journal.

Dipoles localized at helix termini of proteins stabilize charges.

H Luecke, F A Quiocho, F. Quiocho, 1991, Proceedings of the National Academy of Sciences of the United States of America.

Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor.

F A Quiocho, F. Quiocho, L. Rodseth, 1997, Structure.

Mutation of TDP1, encoding a topoisomerase I–dependent DNA damage repair enzyme, in spinocerebellar ataxia with axonal neuropathy

J. Lupski, F. Quiocho, C. Boerkoel, 2002, Nature Genetics.

Refined 1.89-A structure of the histidine-binding protein complexed with histidine and its relationship with many other active transport/chemosensory proteins.

F. Quiocho, N. Yao, S. Trakhanov, 1994, Biochemistry.

Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes

F. Quiocho, P. Ledvina, 1996, Molecular microbiology.

Ligand-free and -bound structures of the binding protein (LivJ) of the Escherichia coli ABC leucine/isoleucine/valine transport system: trajectory and dynamics of the interdomain rotation and ligand specificity.

F. Quiocho, D. Kristensen, Jianpeng Ma, 2005, Biochemistry.

The structure of carboxypeptidase A. IX. The x-ray diffraction results in the light of the chemical sequence.

G. Reeke, F. Quiocho, W. Lipscomb, 1969, Proceedings of the National Academy of Sciences of the United States of America.

Carboxypeptidase A: a protein and an enzyme.

F A Quiocho, F. Quiocho, W. Lipscomb, 1971, Advances in protein chemistry.

Stabilization of charges on isolated ionic groups sequestered in proteins by polarized peptide units

Florante A. Quiocho, F. Quiocho, N. Vyas, 1987, Nature.

Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex.

F A Quiocho, F. Quiocho, A. Means, 1992, Science.

Atomic structures of periplasmic binding proteins and the high-affinity active transport systems in bacteria.

F A Quiocho, F. Quiocho, 1990, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

Structure of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca(v)1.2 calcium channel.

F. Quiocho, S. Hamilton, Susan L Hamilton, 2005, Structure.

Crystal Structure of the VHS and FYVE Tandem Domains of Hrs, a Protein Involved in Membrane Trafficking and Signal Transduction

Florante A. Quiocho, Mark N. Wu, F. Quiocho, 2000, Cell.

Protein-carbohydrate interactions: basic molecular features

F. Quiocho, 1989 .

Atomic interactions in protein-carbohydrate complexes. Tryptophan residues in the periplasmic maltodextrin receptor for active transport and chemotaxis.

F A Quiocho, F. Quiocho, L. Rodseth, 1992, Journal of molecular biology.

A molecular dynamics study of thermodynamic and structural aspects of the hydration of cavities in proteins

Michael H. Mazor, J A McCammon, F A Quiocho, 1991, Biopolymers.

V-ATPase V0 Sector Subunit a1 in Neurons Is a Target of Calmodulin*

P. Hiesinger, F. Quiocho, H. Bellen, 2008, Journal of Biological Chemistry.

Molecular recognition of oligosaccharide epitopes by a monoclonal Fab specific for Shigella flexneri Y lipopolysaccharide: X-ray structures and thermodynamics.

Margaret A. Johnson, M. N. Vyas, F. Quiocho, 2002, Biochemistry.

Fine tuning the specificity of the periplasmic phosphate transport receptor. Site-directed mutagenesis, ligand binding, and crystallographic studies.

F. Quiocho, P. Ledvina, Z. Wang, 1994, The Journal of biological chemistry.

Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110.

F. Quiocho, D. Borhani, J. Petrash, 1993, The Journal of biological chemistry.

1.7 A structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor.

F. Quiocho, T. Nakano, J. Petrash, 1995, Biochemistry.

The calcium-binding site in the galactose chemoreceptor protein. Crystallographic and metal-binding studies.

F A Quiocho, M. N. Vyas, F. Quiocho, 1989, The Journal of biological chemistry.

Mycobacterium tuberculosis 16-kDa Antigen (Hsp16.3) Functions as an Oligomeric Structure in Vitro to Suppress Thermal Aggregation (*)

F. Quiocho, W. Chiu, J. Jakana, 1996, The Journal of Biological Chemistry.

Dynamin-SNARE interactions control trans-SNARE formation in intracellular membrane fusion

F. Quiocho, A. Mayer, K. Ayscough, 2013, Nature Communications.

Atomic basis of the exquisite specificity of phosphate and sulfate transport receptors.

F. Quiocho, 1996, Kidney international.

Aldose Reductase Catalysis and Crystallography: Insights From Recent Advances in Enzyme Structure and Function

F. Quiocho, David K Wilson, J. Petrash, 1994, Diabetes.

The structure of D-galactose-binding protein at 4.1 A resolution looks like L-arabinose-binding protein.

F. Quiocho, J. Pflugrath, 1980, The Journal of biological chemistry.

Preliminary crystallographic data of receptors for transport and chemotaxis in Escherichia coli: D-galactose and maltose-binding proteins.

F. Quiocho, J. Pflugrath, W. E. Meador, 1979, Journal of molecular biology.

Crystallographic and chemical studies of the L-arabinose-binding protein from E. coli.

F. Quiocho, G. Gilliland, D. Miller, 1977, Journal of supramolecular structure.

Refined 2.5 A structure of murine adenosine deaminase at pH 6.0.

F. Quiocho, A. Sharff, D. Wilson, 1992, Journal of molecular biology.

Ca2+–Calmodulin regulates SNARE assembly and spontaneous neurotransmitter release via v-ATPase subunit V0a1

P. Hiesinger, F. Quiocho, W. R. Williamson, 2014, The Journal of cell biology.

Ca 2 + – Calmodulin regulates SNARE assembly and spontaneous neurotransmitter release via v-ATPase subunit V 0 a 1

P. Hiesinger, F. Quiocho, W. R. Williamson, 2014 .

Structural features of the aldose reductase and aldehyde reductase inhibitor-binding sites.

F A Quiocho, F. Quiocho, O. El-Kabbani, 1998, Molecular vision.

A pre-transition-state mimic of an enzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water.

F A Quiocho, F. Quiocho, David K Wilson, 1993, Biochemistry.

The role of divalent cations in structure and function of murine adenosine deaminase

F. Quiocho, F. Rudolph, David K Wilson, 1997, Protein science : a publication of the Protein Society.

Crystallographic observation of a trapped tetrahedral intermediate in a metalloenzyme

F. Quiocho, David K Wilson, 1994, Nature Structural Biology.

Preliminary X-ray analysis of crystals of murine adenosine deaminase.

F. Quiocho, M. Harrison, R. Kellems, 1988, Journal of molecular biology.

The Structure and Function of Intein-Associated Homing Endonucleases

F. Quiocho, Carmen M. Moure, C. M. Moure, 2005 .

Probing the Structure of the PI-SceI-DNA Complex by Affinity Cleavage and Affinity Photocross-linking*

F. Quiocho, M. Crist, X. Duan, 2000, The Journal of Biological Chemistry.

Inhibitors of sterol synthesis. Chemical synthesis, structure, and biological activities of (25R)-3 beta,26-dihydroxy-5 alpha-cholest-8(14)-en-15-one, a metabolite of 3 beta-hydroxy-5 alpha-cholest-8(14)-en-15-one.

W. K. Wilson, F. Quiocho, H. S. Kim, 1989, Journal of lipid research.

Crystal structure of the cytoplasmic N-terminal domain of subunit I, a homolog of subunit a, of V-ATPase.

F. Quiocho, M. Baker, N. Vyas, 2011, Journal of molecular biology.

Man bites dog

F. Quiocho, W. E. Meador, 2002, Nature Structural Biology.

Sorting of the Yeast Vacuolar-type, Proton-translocating ATPase Enzyme Complex (V-ATPase)

Gregory C. Finnigan, F. Quiocho, T. Stevens, 2012, The Journal of Biological Chemistry.

Schimke immuno-osseous dysplasia: SMARCAL1 loss-of-function and phenotypic correlation

F. Quiocho, A. Baradaran‐Heravi, K. Choi, 2008, Journal of Medical Genetics.

Specifically Targeted Modification of Human Aldose Reductase by Physiological Disulfides*

F. Quiocho, M. Dal Monte, A. Del Corso, 1996, The Journal of Biological Chemistry.

Crystal Structure of PI-SceI, a Homing Endonuclease with Protein Splicing Activity

F. Quiocho, X. Duan, Xiaoqun Duan, 1997, Cell.

Structure of the Pho85-Pho80 CDK-cyclin complex of the phosphate-responsive signal transduction pathway.

E. O’Shea, F. Quiocho, G. Leonard, 2007, Molecular cell.

Crystallization and preliminary x‐ray crystallographic analysis of the 38‐kda immunodominant antigen of mycobacterium tuberculosis

M. N. Vyas, F. Quiocho, N. Vyas, 1994, Protein Science.

Preliminary crystallographic analysis of the Fab fragment of an antibody against HIV gp120.

M. N. Vyas, F. Quiocho, N. Vyas, 1990, Journal of molecular biology.

Preliminary crystallographic data for a leucine, isoleucine, valine-binding protein from Escherichia coli K12.

F. Quiocho, W. E. Meador, 1978, Journal of molecular biology.

Leucine/isoleucine/valine-binding protein contracts upon binding of ligand.

F. Quiocho, J. Trewhella, G. Olah, 1993, The Journal of biological chemistry.

Immobilized proteins in single crystals.

F. Quiocho, 1976, Methods in enzymology.

The structure of concanavalin A at 4 A resolution.

G. Reeke, F. Quiocho, J. W. Becker, 1971, Cold Spring Harbor symposia on quantitative biology.

THE ACTION OF ANHYDROUS ACIDS ON ATP:CREATINE PHOSPHOTRANSFERASE

F. Quiocho, F. Friedberg, 1962 .

PI-SCEI, A HOMING ENDONUCLEASE WITH PROTEIN SPLICING ACTIVITY

F. Quiocho, X. Duan, 1998 .

The "cap-binding slot" of an mRNA cap-binding protein: quantitative effects of aromatic side chain choice in the double-stacking sandwich with cap.

F. Quiocho, P. Gershon, Changzheng Li, 2002, Biochemistry.

Recognition of capped RNA substrates by VP39, the vaccinia virus-encoded mRNA cap-specific 2'-O-methyltransferase.

F. Quiocho, S. W. Lockless, A. Hodel, 1998, Biochemistry.

L-Arabinose-binding protein-sugar complex at 2.4 A resolution. Stereochemistry and evidence for a structural change.

F. Quiocho, G. Gilliland, M. Newcomer, 1981, Journal of Biological Chemistry.

The structure of carboxypeptidase a, vi. Some results at 2.0-a resolution, and the complex with glycyl-tyrosine at 2.8-a resolution.

G. Reeke, T. Steitz, F. Quiocho, 1967, Proceedings of the National Academy of Sciences of the United States of America.

X-ray diffraction and nuclear magnetic resonance dispersion studies on derivatives of carboxypeptidase A.

F. Quiocho, W. Lipscomb, P. Bethge, 1972, Cold Spring Harbor symposia on quantitative biology.

Making of the minibody

F. Quiocho, 1993, Nature.

Predicted structure of the sugar-binding site of the lac repressor

F. Quiocho, N. Vyas, K. Matthews, 1984, Nature.

Crystal structure of FAS thioesterase domain with polyunsaturated fatty acyl adduct and inhibition by dihomo-γ-linolenic acid

Wei Zhang, B. Chakravarty, Ziwei Gu, 2011, Proceedings of the National Academy of Sciences.

Carbohydrate-binding proteins: tertiary structures and protein-sugar interactions.

F A Quiocho, F. Quiocho, 1986, Annual review of biochemistry.

A nonconservative serine to cysteine mutation in the sulfate-binding protein, a transport receptor.

F. Quiocho, J. He, J. J. He, 1991, Science.

High specificity of a phosphate transport protein determined by hydrogen bonds

F. Quiocho, H. Luecke, 1990, Nature.

Structural studies of aldo-keto reductase inhibition.

F. Quiocho, T. Nakano, J. Petrash, 1997, Advances in experimental medicine and biology.

Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat.

F A Quiocho, F. Quiocho, D K Wilson, 1993, Proceedings of the National Academy of Sciences of the United States of America.

An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications.

F A Quiocho, F. Quiocho, K. Bohren, 1992, Science.

Sulphate sequestered in the sulphate-binding protein of Salmonella typhimurium is bound solely by hydrogen bonds

F. Quiocho, J. Pflugrath, 1985, Nature.

The Enzymic Behavior of Carboxypeptidase-A in the Solid State*

F. Richards, F. Quiocho, 1966 .

The structure of carboxypeptidase A. 8. Atomic interpretation at 0.2 nm resolution, a new study of the complex of glycyl-L-tyrosine with CPA, and mechanistic deductions.

G N Reeke, F A Quiocho, G. Reeke, 1970, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

The structure of carboxypepidase A. V. Studies of enzyme-substrate and enzyme-inhibitor complexes at 6 A resolution.

F A Quiocho, T. Steitz, F. Quiocho, 1967, The Journal of biological chemistry.

Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2-A resolution.

J S Sack, F A Quiocho, F. Quiocho, 1992, The Journal of biological chemistry.

The 2 A resolution structure of the sulfate-binding protein involved in active transport in Salmonella typhimurium.

F A Quiocho, F. Quiocho, J. Pflugrath, 1988, Journal of molecular biology.

Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor.

F. Quiocho, N. Yao, P. Ledvina, 1996, Biochemistry.

Sulfate-binding protein dislikes protonated oxyacids. A molecular explanation.

F. Quiocho, B. Jacobson, Bruce L. Jacobson, 1988, Journal of molecular biology.

Protein–ligand interactions

F. Quiocho, A. Hodel, 2012 .

Crystal structure of M tuberculosis ABC phosphate transport receptor: specificity and charge compensation dominated by ion-dipole interactions.

M. N. Vyas, F. Quiocho, N. Vyas, 2003, Structure.

Dominant role of local dipolar interactions in phosphate binding to a receptor cleft with an electronegative charge surface: Equilibrium, kinetic, and crystallographic studies

F. Quiocho, P. Ledvina, A. Tsai, 1998, Protein science : a publication of the Protein Society.

A low energy short hydrogen bond in very high resolution structures of protein receptor-phosphate complexes

F. Quiocho, H. Luecke, N. Yao, 1997, Nature Structural Biology.

Dominant role of local dipoles in stabilizing uncompensated charges on a sulfate sequestered in a periplasmic active transport protein

F. Quiocho, Florante A. Quiocho, Jing J. He, 1993, Protein science : a publication of the Protein Society.

Interdomain salt bridges modulate ligand-induced domain motion of the sulfate receptor protein for active transport.

F. Quiocho, D. Lemon, B. Jacobson, 1992, Journal of molecular biology.

Atomic structures and function of periplasmic receptors for active transport and chemotaxis

F. Quiocho, 1991 .

Substrate specificity and affinity of a protein modulated by bound water molecules

F. A. Quiocho, F. Quiocho, N. Vyas, 1989, Nature.

A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis

Florante A. Quiocho, M. N. Vyas, F. Quiocho, 1987, Nature.

Crystallization and x-ray diffraction studies of a phosphate-binding protein involved in active transport in Escherichia coli.

F. Quiocho, H. Luecke, H. Rosenberg, 1986, Journal of Biological Chemistry.

Novel stereospecificity of the L-arabinose-binding protein

Florante A. Quiocho, F. Quiocho, N. Vyas, 1984, Nature.

Periplasmic binding protein structure and function. Refined X-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine.

F. Quiocho, J. Sack, M. Saper, 1989, Journal of molecular biology.

Comparison of the periplasmic receptors for L-arabinose, D-glucose/D-galactose, and D-ribose. Structural and Functional Similarity.

F A Quiocho, M. N. Vyas, F. Quiocho, 1991, The Journal of biological chemistry.

Refined 1.8-A structure reveals the mode of binding of beta-cyclodextrin to the maltodextrin binding protein.

F A Quiocho, F. Quiocho, A. Sharff, 1993, Biochemistry.

Calmodulin structure refined at 1.7 A resolution.

F A Quiocho, F. Quiocho, A. Means, 1992, Journal of molecular biology.

Structure of the L-leucine-binding protein refined at 2.4 A resolution and comparison with the Leu/Ile/Val-binding protein structure.

F. Quiocho, J. Sack, S. Trakhanov, 1989, Journal of molecular biology.

Structure of the L-arabinose-binding protein from Escherichia coli at 2.4 A resolution.

G L Gilliland, F A Quiocho, F. Quiocho, 1980, Journal of molecular biology.

Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis.

F A Quiocho, F. Quiocho, J. Pflugrath, 1983, The Journal of biological chemistry.

The mechanism of sugar binding to the periplasmic receptor for galactose chemotaxis and transport in Escherichia coli.

F A Quiocho, F. Quiocho, J. Olson, 1980, The Journal of biological chemistry.

Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures.

F A Quiocho, F. Quiocho, A. Means, 1993, Science.

Functional Consequences of Truncating Amino Acid Side Chains Located at a Calmodulin-Peptide Interface*

F. Quiocho, A. Means, D. J. Sloan, 1997, The Journal of Biological Chemistry.

The 1.85 Å Structure of Vaccinia Protein VP39: A Bifunctional Enzyme That Participates in the Modification of Both mRNA Ends

F. Quiocho, A. Hodel, P. Gershon, 1996, Cell.

Structural Characterization of the UL25 DNA-Packaging Protein from Herpes Simplex Virus Type 1

F. Quiocho, V. Preston, B. R. Bowman, 2006, Journal of Virology.

Concerning the structure of 7α,15β-dichloro-5α-cholest-8(14)-en-3β-ol, a novel inhibitor of cholesterol biosynthesis

F. Quiocho, G. Gilliland, M. Newcomer, 1980 .

Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations.

F A Quiocho, F. Quiocho, F. Rudolph, 1991, Science.

The reaction of creatine kinase with 2-chloromercuri-4-nitrophenol.

F. Quiocho, J. Olson, 1974, The Journal of biological chemistry.

Spectrochemical and ligand-binding studies of an active mercurinitrophenol-labeled creatine kinase.

F. Quiocho, M. Laue, 1977, Biochemistry.

Protein-ligand energetics assessed using deoxy and fluorodeoxy sugars in equilibrium binding and high resolution crystallographic studies.

F. Quiocho, J. Tesmer, P. Vermersch, 1992, Journal of molecular biology.

Probing the functional role of two conserved active site aspartates in mouse adenosine deaminase.

F A Quiocho, F. Quiocho, R. Kellems, 1996, Biochemistry.

Probing the atomic interactions between proteins and carbohydrates.

F. Quiocho, 1993, Biochemical Society transactions.

Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH of maximum activity.

F A Quiocho, F. Quiocho, Z Wang, 1998, Biochemistry.

Identification and removal of colanic acid from plasmid DNA preparations: implications for gene therapy

F. Quiocho, K. Worley, N. Templeton, 2010, Gene Therapy.

Theoretical study of inhibition of adenosine deaminase by (8R)-coformycin and (8R)-deoxycoformycin.

T. Straatsma, F. Quiocho, J. Briggs, 1996, Journal of medicinal chemistry.

New Structural Insights into Phosphorylation-free Mechanism for Full Cyclin-dependent Kinase (CDK)-Cyclin Activity and Substrate Recognition*

F. Quiocho, F. Zheng, 2013, The Journal of Biological Chemistry.

Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase/prolidase.

Saumil S. Shah, F. Quiocho, N. Vyas, 2010, Biochemistry.

Ion–dipole interactions and their functions in proteins

F. Quiocho, K. Sippel, Katherine H. Sippel, 2015, Protein science : a publication of the Protein Society.

Coordination and Stability of Calcium-Binding Site: D-Galactose/D-Glucose-Binding Protein of Bacterial Active Transport and Chemotaxis System

M. N. Vyas, F. Quiocho, N. Vyas, 1991 .

Structural basis of peptide–carbohydrate mimicry in an antibody-combining site

M. N. Vyas, F. Quiocho, N. Vyas, 2003, Proceedings of the National Academy of Sciences of the United States of America.

A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle.

F. Quiocho, Jue Chen, A. Davidson, 2003, Molecular cell.

Trapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport.

F. Quiocho, J. Chen, Jue Chen, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Crystal structure of dimeric cardiac L-type calcium channel regulatory domains bridged by Ca2+·calmodulins

F. Quiocho, M. R. Baker, S. Hamilton, 2009, Proceedings of the National Academy of Sciences.

Discovering Thiamine Transporters as Targets of Chloroquine Using a Novel Functional Genomics Strategy

F. Quiocho, Wei Li, Xuewen Pan, 2012, PLoS genetics.

Crystal structure of the intein homing endonuclease PI-SceI bound to its recognition sequence

F. Quiocho, Carmen M. Moure, F. S. Gimble, 2002, Nature Structural Biology.

The interaction of tetraiodofluorescein with creatine kinase.

F. Quiocho, L. Somerville, 1977, Biochimica et Biophysica Acta.

Crystal structures of the vaccinia virus polyadenylate polymerase heterodimer: insights into ATP selectivity and processivity.

F. Quiocho, B. R. Bowman, P. Gershon, 2006, Molecular cell.

A Novel All Helix Fold of the AP180 Amino-Terminal Domain for Phosphoinositide Binding and Clathrin Assembly in Synaptic Vesicle Endocytosis

F. Quiocho, Jue Chen, Y. Mao, 2001, Cell.

Influence of divalent cations in protein crystallization

F. Quiocho, S. Trakhanov, 1995, Protein science : a publication of the Protein Society.

Crystal structures of the maltodextrin/maltose-binding protein complexed with reduced oligosaccharides: flexibility of tertiary structure and ligand binding.

F A Quiocho, F. Quiocho, H. Nikaido, 2001, Journal of molecular biology.

F. Quiocho, W. Lipscomb, C. McMurray, 1972, Proceedings of the National Academy of Sciences of the United States of America.

Dinucleotide fold proteins. Interaction of arabinose binding protein with Cibacron Blue 3G-A.

F. Quiocho, R. Beissner, F. Rudolph, 1979, Journal of molecular biology.

Multipurpose MRG domain involved in cell senescence and proliferation exhibits structural homology to a DNA-interacting domain.

F. Quiocho, B. R. Bowman, K. Tominaga, 2006, Structure.

Structural basis of mRNA cap recognition by proteins.

F. Quiocho, P. Gershon, G. Hu, 2000, Current opinion in structural biology.

Molecular features and basic understanding of protein-carbohydrate interactions: the arabinose-binding protein-sugar complex.

F. Quiocho, 1988, Current topics in microbiology and immunology.

Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo

Sunil Q. Mehta, F. Quiocho, H. Bellen, 2005, Nature Structural &Molecular Biology.

Sec 15 interacts with Rab 11 via a novel domain and affects Rab 11 localization in vivo

Sunil Q. Mehta, F. Quiocho, H. Bellen, 2005 .

A closed compact structure of native Ca(2+)-calmodulin.

F. Quiocho, Florante A Quiocho, Jennifer L Fallon, 2003, Structure.

Structural basis for sequence-nonspecific recognition of 5'-capped mRNA by a cap-modifying enzyme.

F A Quiocho, F. Quiocho, A. Hodel, 1998, Molecular cell.

Specific protein recognition of an mRNA cap through its alkylated base

F. Quiocho, A. Hodel, P. Gershon, 1997, Nature Structural Biology.

Structural Insights into the Protein Splicing Mechanism of PI-SceI*

F A Quiocho, F. Quiocho, Ming-Qun Xu, 2000, The Journal of Biological Chemistry.

Amino Acid Residues in Both the Protein Splicing and Endonuclease Domains of the PI-SceI Intein Mediate DNA Binding*

F. Quiocho, M. Crist, X. Duan, 1998, The Journal of Biological Chemistry.

[38] Immobilized proteins in single crystals

F. Quiocho, 1976 .

Genetic approach to the role of tryptophan residues in the activities and fluorescence of a bacterial periplasmic maltose-binding protein.

F. Quiocho, M. Hofnung, J. Spurlino, 1990, Journal of molecular biology.

Progress in the identification of interaction sites on the periplasmic maltose binding protein from E coli.

F. Quiocho, M. Hofnung, W. Saurin, 1990, Biochimie.

Computational and biochemical identification of a nuclear pore complex binding site on the nuclear transport carrier NTF2.

F. Quiocho, O. Lichtarge, M. Sowa, 2004, Journal of molecular biology.

Live-Cell Imaging in Caenorhabditis elegans Reveals the Distinct Roles of Dynamin Self-Assembly and Guanosine Triphosphate Hydrolysis in the Removal of Apoptotic Cells

F. Quiocho, Y. Etzion, D. Danino, 2010, Molecular biology of the cell.

The 2.8-A resolution structure of the L-arabinose-binding protein from Escherichia coli. Polypeptide chain folding, domain similarity, and probable location of sugar-binding site.

G L Gilliland, F A Quiocho, F. Quiocho, 1977, The Journal of biological chemistry.

The structure of a calmodulin mutant with a deletion in the central helix: implications for molecular recognition and protein binding.

F. Quiocho, A. Means, L. Tabernero, 1997, Structure.

X-ray analysis reveals conformational adaptation of the linker in functional calmodulin mutants

F. Quiocho, A. Means, S. George, 1995, Nature Structural Biology.

Twitching worms catch S100

F. Quiocho, K. Johnson, 1996, Nature.

Structure of L-arabinose-binding protein from Escherichia coli at 5 A resolution and preliminary results at 3.5 A.

F. Quiocho, G. Phillips, V. Mahajan, 1976, Proceedings of the National Academy of Sciences of the United States of America.

Novel tertiary structures and stereospecificities of periplasmic binding proteins involved in active transport and chemotaxis

M. N. Vyas, F. Quiocho, N. Vyas, 1985, Journal of Biosciences.

Periplasmic Binding Proteins: Structures and New Understanding of Protein-Ligand Interactions

F. Quiocho, N. Vyas, J. Sack, 1987 .

Normal mode refinement of anisotropic thermal parameters for a supramolecular complex at 3.42-Å crystallographic resolution

Jianpeng Ma, Billy K Poon, Xiaorui Chen, 2007, Proceedings of the National Academy of Sciences.

mRNA cap recognition: dominant role of enhanced stacking interactions between methylated bases and protein aromatic side chains.

F A Quiocho, F. Quiocho, A. Hodel, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Hinge-bending in L-arabinose-binding protein. The "Venus's-flytrap" model.

J A McCammon, F A Quiocho, F. Quiocho, 1982, The Journal of biological chemistry.

Leucine, isoleucine, valine-binding protein from Escherichia coli. Structure at 3.0-A resolution and location of the binding site.

F. Quiocho, M. Saper, 1983, The Journal of biological chemistry.

Sterol biosynthesis: Establishment of the structure of 3β-p-bromobenzoyloxy-5α-cholest-8(14)-en-15β-ol

F. Quiocho, G. Phillips, R. Sass, 1976 .

INTERMOLECULAR CROSS LINKING OF A PROTEIN IN THE CRYSTALLINE STATE: CARBOXYPEPTIDASE-A.

F. Richards, F. Quiocho, 1964, Proceedings of the National Academy of Sciences of the United States of America.

Insertion of an N7-methylguanine mRNA Cap between Two Coplanar Aromatic Residues of a Cap-binding Protein Is Fast and Selective for a Positively Charged Cap*

Florante A. Quiocho, F. Quiocho, A. Tsai, 2003, Journal of Biological Chemistry.

Thermodynamics of the binding of L-arabinose and of D-galactose to the L-arabinose-binding protein of Escherichia coli.

J M Sturtevant, F A Quiocho, F. Quiocho, 1983, The Journal of biological chemistry.

Stereospecificity of creatine kinase. Crystal structure of 1-carboxymethyl-2-imino-3-phosphonoimidazolidine

F. Quiocho, T. Annesley, G. Phillips, 1979 .

Preliminary time-of-flight neutron diffraction studies of Escherichia coli ABC transport receptor phosphate-binding protein at the Protein Crystallography Station.

F. Quiocho, J. Bacik, S. Z. Fisher, 2014, Acta crystallographica. Section F, Structural biology communications.

Crystal Structure of the Human Fatty Acid Synthase Enoyl-Acyl Carrier Protein-Reductase Domain Complexed with Triclosan Reveals Allosteric Protein-Protein Interface Inhibition*

F. Quiocho, N. Vyas, B. Sankaran, 2014, The Journal of Biological Chemistry.

Crystal structure of a catalytic intermediate of the maltose transporter

F. Quiocho, Jue Chen, A. Davidson, 2007, Nature.

Molecular basis of cyclin-CDK-CKI regulation by reversible binding of an inositol pyrophosphate.

E. O’Shea, F. Quiocho, Kexin Huang, 2008, Nature chemical biology.

The crystal structure of the gene targeting homing endonuclease I-SceI reveals the origins of its target site specificity.

F. Quiocho, Frederick S Gimble, Florante A Quiocho, 2003, Journal of molecular biology.

CHAIN: a crystallographic modeling program.

J S Sack, F A Quiocho, F. Quiocho, 1997, Methods in enzymology.

Negative electrostatic surface potential of protein sites specific for anionic ligands.

F. Quiocho, N. Yao, P. Ledvina, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Concerning the structure of 3β-benzoyloxy-5β-cholesta-8,14-diene, a major byproduct in the chemical synthesis of 5α-cholest-8(14)-en-3β-ol-15-one

W. K. Wilson, F. Quiocho, David K Wilson, 1988 .

VHS domain – a longshoreman of vesicle lines

Veli Pekka Lehto, Olli Lohi, F. Quiocho, 2002, FEBS letters.

Location of the sugar-binding site of L-arabinose-binding protein. Sugar derivative syntheses, sugar binding specificity, and difference Fourier analyses.

F A Quiocho, F. Quiocho, M. Newcomer, 1979, The Journal of biological chemistry.

Site-directed mutagenesis of histidine 238 in mouse adenosine deaminase: substitution of histidine 238 does not impede hydroxylate formation.

F A Quiocho, F. Quiocho, F. Rudolph, 1996, Biochemistry.

2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor.

F. Quiocho, A. Nickitenko, S. Trakhanov, 1995, Biochemistry.

A thermodynamic study of the binding of linear and cyclic oligosaccharides to the maltodextrin-binding protein of Escherichia coli.

J M Sturtevant, F A Quiocho, F. Quiocho, 1998, Biophysical chemistry.

Conservative and nonconservative mutations in proteins: Anomalous mutations in a transport receptor analyzed by free energy and quantum chemical calculations

F. Quiocho, J. Briggs, J. Mccammon, 1995, Protein science : a publication of the Protein Society.

A Pro to Gly mutation in the hinge of the arabinose-binding protein enhances binding and alters specificity. Sugar-binding and crystallographic studies.

F A Quiocho, F. Quiocho, D. Lemon, 1992, The Journal of biological chemistry.

Crystallization of genetically engineered active maltose-binding proteins, including an immunogenic viral epitope insertion.

F. Quiocho, M. Hofnung, L. Rodseth, 1990, Journal of Molecular Biology.

Inhibitors of sterol synthesis. Concerning the structure of 15β-methyl-5α,14β-cholest-7-ene-3β,15α-diol, an inhibitor of cholesterol biosynthesis

W. K. Wilson, F. Quiocho, E. Parish, 1988 .

Synthesis and structure of 15-oxygenated 5α,14β-cholest-7-en-3β-ol derivatives

F. Quiocho, G. Gilliland, M. Newcomer, 1976 .

Identification of Lys-403 in the PI-SceI Homing Endonuclease as Part of a Symmetric Catalytic Center*

F. Quiocho, X. Duan, F. S. Gimble, 1998, The Journal of Biological Chemistry.

Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose and D-galactose.

M. N. Vyas, F. Quiocho, N. Vyas, 1994, Biochemistry.

Molecular graphics abstractsMolecular modelling with the PS 300: a new generation graphics display system

J. W. Pflugrath, M. A. Saper, F. A. Quiocho, 1983 .

Determinants in CaV1 Channels That Regulate the Ca2+ Sensitivity of Bound Calmodulin*

F. Quiocho, Dimitra K. Georgiou, S. Hamilton, 2009, The Journal of Biological Chemistry.

Structural evidence for a dominant role of nonpolar interactions in the binding of a transport/chemosensory receptor to its highly polar ligands.

Florante A. Quiocho, F. Quiocho, X. Duan, 2002, Biochemistry.

The 3 A resolution structure of a D-galactose-binding protein for transport and chemotaxis in Escherichia coli.

M. N. Vyas, F. Quiocho, N. Vyas, 1983, Proceedings of the National Academy of Sciences of the United States of America.

Crystal structures of I-SceI complexed to nicked DNA substrates: snapshots of intermediates along the DNA cleavage reaction pathway

Florante A. Quiocho, F. Quiocho, Frederick S. Gimble, 2008, Nucleic acids research.

Structure of the bifunctional and Golgi‐associated formiminotransferase cyclodeaminase octamer

Wah Chiu, Steven J Ludtke, Dong-Hua Chen, 2004, The EMBO journal.

The radius of gyration of L-arabinose-binding protein decreases upon binding of ligand.

F A Quiocho, F. Quiocho, B. Lewis, 1981, The Journal of biological chemistry.

Preliminary crystallographic analysis of a Fab specific for the O-antigen of Shigella flexneri cell surface lipopolysaccharide with and without bound saccharides.

M. N. Vyas, F. Quiocho, P. Meikle, 1993, Journal of molecular biology.

N-bromosuccinimide action on creatine phosphokinase

F. Quiocho, F. Friedberg, M. O'Dell, 1961, Experientia.

Atomic protein structures reveal basic features of binding of sugars and ionic substrates, and calcium cation.

M. N. Vyas, F. Quiocho, N. Vyas, 1987, Cold Spring Harbor Symposia on Quantitative Biology.

Molecular docking study of the interactions between the thioesterase domain of human fatty acid synthase and its ligands

Jianpeng Ma, Qinghua Wang, F. Quiocho, 2008, Proteins.

The immunodominant 38-kDa lipoprotein antigen of Mycobacterium tuberculosis is a phosphate-binding protein.

F. Quiocho, R. Lathigra, A. Choudhary, 1994, The Journal of biological chemistry.

References and Notes Supporting Online Material Materials and Methods Figs. S1 to S3 Table S1 References Antibody Class Switching Mediated by Yeast Endonuclease–generated Dna Breaks

Frederick W. Alt, F. Alt, F. Quiocho, 2022 .

Engineered interdomain disulfide in the periplasmic receptor for sulfate transport reduces flexibility. Site-directed mutagenesis and ligand-binding studies.

F A Quiocho, F. Quiocho, D. Lemon, 1991, The Journal of biological chemistry.

Sugar-binding and crystallographic studies of an arabinose-binding protein mutant (Met108Leu) that exhibits enhanced affinity and altered specificity.

F A Quiocho, F. Quiocho, D. Lemon, 1991, Biochemistry.

Inversion of receptor binding preferences by mutagenesis: free energy thermodynamic integration studies on sugar binding to L-arabinose binding proteins.

T. Straatsma, F. Quiocho, M. Zacharias, 1993, Biochemistry.

The Removal and Exchange of Metal Ions in Cross-Linked Crystals of Carboxypeptidase-A*

F. Richards, F. Quiocho, W. Bishop, 1966 .

Protein–ligand interactions

F. Quiocho, A. Hodel, 2012 .

Model of lactose repressor core based on alignment with sugar-binding proteins is concordant with genetic and chemical data.

F. Quiocho, N. Vyas, K. Matthews, 1993, Journal of Biological Chemistry.

The thiol group of the L-arabinose-binding protein. Chromophoric labeling and chemical identification of the sugar-binding site.

F. Quiocho, M. Newcomer, D. Miller, 1979, The Journal of biological chemistry.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES.

E. B. Wilson, F. Quiocho, V. I, 1916, Science.

Crystallographic data of an l-arabinose-binding protein from Escherichia coli

Robert W. Hogg, Florante A. Quiocho, F. Quiocho, 1974 .

The structure of carboxypeptidase A. VII. The 2.0-angstrom resolution studies of the enzyme and of its complex with glycyltyrosine, and mechanistic deductions.

G. Reeke, T. Steitz, F. Quiocho, 1968, Brookhaven symposia in biology.

7alpha, 15beta-Dichloro-5alpha-cholest-8 (14)-en-3beta-ol, a novel inhibitor of sterol biosynthesis in animal cells.

F. Quiocho, G. Gilliland, M. Newcomer, 1978, Biochemical and biophysical research communications.