about
Stabilization and characterization of a heme-oxy reaction intermediate in inducible nitric-oxide synthaseStructural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2Backbone structure of a small helical integral membrane protein: A unique structural characterizationStructure of an integrin IIb 3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activationExpression, purification and structural characterization of functionally replete thrombospondin-1 type 1 repeats in a bacterial expression systemStructural Characterization of Carbohydrate Binding by LMAN1 Protein Provides New Insight into the Endoplasmic Reticulum Export of Factors V (FV) and VIII (FVIII)Crystal structure of the nucleotide-binding domain of mortalin, the mitochondrial Hsp70 chaperoneInvestigating the Impact of Polymer Functional Groups on the Stability and Activity of Lysozyme-Polymer ConjugatesUsing PyMOL to Explore the Effects of pH on Noncovalent Interactions between Immunoglobulin G and Protein A: A Guided-Inquiry Biochemistry Activity.A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteinsDissecting structural and electronic effects in inducible nitric oxide synthaseCrystallization and preliminary X-ray crystallographic analysis of the Bag2 amino-terminal domain from Mus musculusStrategies for Biophysical Characterization of Protein-Polymer Conjugates.Transmembrane helix uniformity examined by spectral mapping of torsion angles.RACK1 interacts with filamin-A to regulate plasma membrane levels of the cystic fibrosis transmembrane conductance regulator.1H, 15N and 13C resonance assignments for free and IEEVD peptide-bound forms of the tetratricopeptide repeat domain from the human E3 ubiquitin ligase CHIP.Biochemical characterization and zinc binding group (ZBGs) inhibition studies on the catalytic domain of MMP7 (cdMMP7).Unraveling the CHIP:Hsp70 complex as an information processor for protein quality control.Clinical Variants of New Delhi Metallo-β-Lactamase Are Evolving To Overcome Zinc Scarcity.Polymer Conjugation to Enhance Cellulase Activity and Preserve Thermal and Functional Stability.Dipicolinic Acid Derivatives as Inhibitors of New Delhi Metallo-β-lactamase-1.Probing the Interaction of Aspergillomarasmine A with Metallo-β-lactamases NDM-1, VIM-2, and IMP-7.Extraction of Thermodynamic Parameters of Protein Unfolding Using Parallelized Differential Scanning Fluorimetry.Approaches for Conjugating Tailor-Made Polymers to Proteins.Design, synthesis and evaluation of XZH-5 analogues as STAT3 inhibitors.Well-Defined Macromolecules Using Horseradish Peroxidase as a RAFT Initiase.Disrupted structure and aberrant function of CHIP mediates the loss of motor and cognitive function in preclinical models of SCAR16Investigating the Mechanism of Horseradish Peroxidase as a RAFT-Initiase.The best of both worlds: active enzymes by grafting-to followed by grafting-from a proteinEvolution of New Delhi metallo-β-lactamase (NDM) in the clinic: Effects of NDM mutations on stability, zinc affinity, and mono-zinc activityToward Next-Generation Biohybrid Catalyst Design: Influence of Degree of Polymerization on Enzyme ActivityCorrection to Dipicolinic Acid Derivatives as Inhibitors of New Delhi Metallo-β-lactamase-11H, 13C, and 15N backbone resonance assignments for KPC-2, a class A serine-β-lactamaseGuided inquiry activity linking thermodynamic parameters of protein unfolding to structure using differential scanning fluorimetry data in the biophysical chemistry classroomA Noncanonical Metal Center Drives the Activity of the Sediminispirochaeta smaragdinae Metallo-β-lactamase SPS-1A Single Salt Bridge in VIM-20 Increases Protein Stability and Antibiotic Resistance under Low-Zinc ConditionsInfluence of substrates and inhibitors on the structure of Klebsiella pneumoniae carbapenemase-22- and N6-functionalized adenosine-5'-diphosphate analogs for the inhibition of mortalinBiophysical Consequences of EVEN-PLUS Syndrome Mutations for the Function of MortalinPolymer conjugation of proteins as a synthetic post-translational modification to impact their stability and activity
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researcher ORCID ID = 0000-0002-3006-3171
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wetenschapper
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name
Richard C Page
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Richard C Page
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Richard C Page
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Richard C Page
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Richard C Page
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Richard C Page
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Richard C Page
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Richard C Page
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Richard C Page
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P106
P31
P496
0000-0002-3006-3171