O. Nadeau

发表

Differential Affinity Cross-linking of Phosphorylase Kinase Conformers by the Geometric Isomers of Phenylenedimaleimide*

D. Sacks, O. Nadeau, G. Carlson, 1997, The Journal of Biological Chemistry.

Expressed phosphorylase b kinase and its alphagammadelta subcomplex as regulatory models for the rabbit skeletal muscle holoenzyme.

D. Walsh, J. Peters, Jessica M. Sage, 2009, Biochemistry.

Ca2+‐induced structural changes in phosphorylase kinase detected by small‐angle X‐ray scattering

J. Trewhella, W. Heller, B. Macdonald, 2005, Protein science : a publication of the Protein Society.

High Functioning Autism with Missense Mutations in Synaptotagmin-Like Protein 4 (SYTL4) and Transmembrane Protein 187 (TMEM187) Genes: SYTL4- Protein Modeling, Protein-Protein Interaction, Expression Profiling and MicroRNA Studies

M. Butler, S. K. Rafi, S. Álvarez, 2019, International journal of molecular sciences.

Protein Structural Analysis via Mass Spectrometry-Based Proteomics.

A. Artigues, M. Villar, Xiuxia Du, 2016, Advances in experimental medicine and biology.

Mass Spectrometric Analysis of Surface-Exposed Regions in the Hexadecameric Phosphorylase Kinase Complex.

A. Artigues, M. Villar, V. Vasquez-Montes, 2015, Biochemistry.

Differential Use of the βL Subunit of the Type I Interferon (IFN) Receptor Determines Signaling Specificity for IFNα2 and IFNβ*

L. Platanias, O. Colamonici, E. Fish, 1998, The Journal of Biological Chemistry.

Dynamic Actions of Glucose and Glucosamine on Hexosamine Biosynthesis in Isolated Adipocytes

S. Marshall, O. Nadeau, K. Yamasaki, 2004, Journal of Biological Chemistry.

Evidence that bismuth salts reduce invasion of epithelial cells by enteroinvasive bacteria

G. Hendricks, O. Nadeau, D. Meyer, 2004, Medical Microbiology and Immunology.

Cryoelectron microscopy reveals new features in the three‐dimensional structure of phosphorylase kinase

E. Gogol, O. Nadeau, G. Carlson, 2005, Protein science : a publication of the Protein Society.

Identification of a Domain in the β Subunit of the Type I Interferon (IFN) Receptor That Exhibits a Negative Regulatory Effect in the Growth Inhibitory Action of Type I IFNs*

B. Neel, L. Platanias, S. Uddin, 1998, Journal of Biological Chemistry.

The regulatory beta subunit of phosphorylase kinase interacts with glyceraldehyde-3-phosphate dehydrogenase.

A. Artigues, M. Villar, Jessica M. Sage, 2008, Biochemistry.

The calmodulin-binding domain of the catalytic gamma subunit of phosphorylase kinase interacts with its inhibitory alpha subunit: evidence for a Ca2+ sensitive network of quaternary interactions.

Qing Yang, O. Nadeau, G. Carlson, 2002, The Journal of biological chemistry.

A region of the beta subunit of the interferon alpha receptor different from box 1 interacts with Jak1 and is sufficient to activate the Jak-Stat pathway and induce an antiviral state.

L. Platanias, O. Colamonici, E. Fish, 1997, The Journal of biological chemistry.

Mass Spectrometry Reveals Differences in Stability and Subunit Interactions between Activated and Nonactivated Conformers of the ( (cid:1)(cid:2)(cid:3)(cid:4) ) 4 Phosphorylase Kinase Complex*

C. Robinson, O. Nadeau, G. Carlson, 2020 .

Mass Spectrometry Reveals Differences in Stability and Subunit Interactions between Activated and Nonactivated Conformers of the (αβγδ)4 Phosphorylase Kinase Complex*

C. Robinson, O. Nadeau, G. Carlson, 2012, Molecular & Cellular Proteomics.

CrossSearch, a User-friendly Search Engine for Detecting Chemically Cross-linked Peptides in Conjugated Proteins*S

Gerald J Wyckoff, Gerald J. Wyckoff, J. Paschall, 2008, Molecular & Cellular Proteomics.

Evidence for the location of the allosteric activation switch in the multisubunit phosphorylase kinase complex from mass spectrometric identification of chemically crosslinked peptides.

Qing Yang, Gerald J Wyckoff, Gerald J. Wyckoff, 2007, Journal of molecular biology.

A review of methods used for identifying structural changes in a large protein complex.

O. Nadeau, G. Carlson, 2012, Methods in molecular biology.

Structural evidence for co-evolution of the regulation of contraction and energy production in skeletal muscle.

A. Artigues, O. Nadeau, G. Carlson, 2008, Journal of molecular biology.

Differential Use of the b L Subunit of the Type I Interferon (IFN) Receptor Determines Signaling Specificity for IFN a 2 and IFN b *

L. Platanias, O. Colamonici, E. Fish, 1998 .

Global miRNA/proteomic analyses identify miRNAs at 14q32 and 3p21, which contribute to features of chronic iron-exposed fallopian tube epithelial cells

Stephanie M. Rockfield, M. Nanjundan, S. Stevens, 2021, Scientific Reports.

The regulation of glycogenolysis in the brain

O. Nadeau, G. Carlson, J. Fontes, 2018, The Journal of Biological Chemistry.

Effects of Combined Phosphorylation at Ser-617 and Ser-1179 in Endothelial Nitric-oxide Synthase on EC50(Ca2+) Values for Calmodulin Binding and Enzyme Activation*

A. Persechini, Q. Tran, D. J. Black, 2009, Journal of Biological Chemistry.

The glucoamylase inhibitor acarbose is a direct activator of phosphorylase kinase.

J. Peters, Jessica M. Sage, O. Nadeau, 2010, Biochemistry.

A Region of the β Subunit of the Interferon α Receptor Different from Box 1 Interacts with Jak1 and Is Sufficient to Activate the Jak-Stat Pathway and Induce an Antiviral State*

L. Platanias, O. Colamonici, E. Fish, 1997, The Journal of Biological Chemistry.

The Proximal Tyrosines of the Cytoplasmic Domain of the β Chain of the Type I Interferon Receptor Are Essential for Signal Transducer and Activator of Transcription (Stat) 2 Activation

D. Levy, L. Platanias, S. Uddin, 1999, The Journal of Biological Chemistry.

Activation of Phosphorylase Kinase by Physiological Temperature.

J. Herrera, O. Nadeau, G. Carlson, 2015, Biochemistry.

Protein Interactions Captured by Chemical Cross-linking: One-Step Cross-linking with Formaldehyde.

O. Nadeau, G. Carlson, 2007, CSH protocols.

Glucosamine-induced Activation of Glycogen Biosynthesis in Isolated Adipocytes

S. Marshall, O. Nadeau, K. Yamasaki, 2005, Journal of Biological Chemistry.

A Ca(2+)-dependent global conformational change in the 3D structure of phosphorylase kinase obtained from electron microscopy.

E. Gogol, O. Nadeau, G. Carlson, 2002, Structure.

The Structural Effects of Endogenous and Exogenous Ca2+/Calmodulin on Phosphorylase Kinase*

D. Sacks, O. Nadeau, G. Carlson, 1997, The Journal of Biological Chemistry.

Structural characterization of the catalytic γ and regulatory β subunits of phosphorylase kinase in the context of the hexadecameric enzyme complex

A. Artigues, O. Nadeau, G. Carlson, 2018, Protein science : a publication of the Protein Society.

Zero-Length Crosslinking of the β Subunit of Phosphorylase Kinase to the N-Terminal Half of its Regulatory α Subunit

O. Nadeau, G. Carlson, K. W. Traxler, 1998 .

Zero length conformation-dependent cross-linking of phosphorylase kinase subunits by transglutaminase.

O. Nadeau, G. Carlson, 1994, Journal of Biological Chemistry.

A model for activation of the hexadecameric phosphorylase kinase complex deduced from zero‐length oxidative crosslinking

O. Nadeau, G. Carlson, Jackie A Thompson, 2015, Protein science : a publication of the Protein Society.

The structure of the large regulatory α subunit of phosphorylase kinase examined by modeling and hydrogen‐deuterium exchange

Yang Zhang, Jianyi Yang, A. Artigues, 2018, Protein science : a publication of the Protein Society.

Structure and Location of the Regulatory β Subunits in the (αβγδ)4 Phosphorylase Kinase Complex* ♦

Yang Zhang, Dong Xu, Qing Yang, 2012, The Journal of Biological Chemistry.

Physicochemical changes in phosphorylase kinase induced by its cationic activator Mg2+

Jessica M. Sage, O. Nadeau, G. Carlson, 2013, Protein science : a publication of the Protein Society.

Site-specific identification and validation of hepatic histone nitration in vivo: Implications for alcohol-induced liver injury.

Nalvi D. Duro, S. Varma, S. Stevens, 2021, Journal of mass spectrometry : JMS.

Deposition of bismuth by Yersinia enterocolitica

G. Hendricks, O. Nadeau, D. Meyer, 2004, Medical Microbiology and Immunology.