about
Rab9 GTPase regulates late endosome size and requires effector interaction for its stability3‘-Phosphoadenosine-5‘-phosphosulfate Reductase in Complex with Thioredoxin: A Structural Snapshot in the Catalytic Cycle † , ‡Regulation of A20 and other OTU deubiquitinases by reversible oxidationChallenges in enzyme mechanism and energeticsFirst-in-Class Inhibitors of Sulfur Metabolism with Bactericidal Activity against Non-Replicating M. tuberculosisInvestigation of the iron-sulfur cluster in Mycobacterium tuberculosis APS reductase: implications for substrate binding and catalysisReengineering redox sensitive GFP to measure mycothiol redox potential of Mycobacterium tuberculosis during infectionSulfenic acid chemistry, detection and cellular lifetimeSpectroscopic studies on the [4Fe-4S] cluster in adenosine 5'-phosphosulfate reductase from Mycobacterium tuberculosis.Site-specific mapping and quantification of protein S-sulphenylation in cells.Redox-based probes as tools to monitor oxidized protein tyrosine phosphatases in living cells.Empirical entropic contributions in computational docking: evaluation in APS reductase complexes.Efficient microwave-assisted solid phase coupling of nucleosides, small library generation and mild conditions for release of nucleoside derivativesCysteine-mediated redox signaling: chemistry, biology, and tools for discoveryNew targets and inhibitors of mycobacterial sulfur metabolism.Geometric and electrostatic study of the [4Fe-4S] cluster of adenosine-5'-phosphosulfate reductase from broken symmetry density functional calculations and extended X-ray absorption fine structure spectroscopy.Design, synthesis and evaluation of Fe-S targeted adenosine 5'-phosphosulfate reductase inhibitors.Substrate recognition, protein dynamics, and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5'-phosphosulfate reductase.A universal entropy-driven mechanism for thioredoxin-target recognition.The Expanding Landscape of the Thiol Redox Proteome.Site-Specific Proteomic Mapping Identifies Selectively Modified Regulatory Cysteine Residues in Functionally Distinct Protein Networks.Profiling the Reactivity of Cyclic C-Nucleophiles towards Electrophilic Sulfur in Cysteine Sulfenic AcidSulforaphane inhibits pancreatic cancer through disrupting Hsp90-p50(Cdc37) complex and direct interactions with amino acids residues of Hsp90.Activity of the tetrapyrrole regulator CrtJ is controlled by oxidation of a redox active cysteine located in the DNA binding domain.Global, in situ, site-specific analysis of protein S-sulfenylationDiverse Redoxome Reactivity Profiles of Carbon Nucleophiles.Light-Mediated Sulfenic Acid Generation from Photocaged Cysteine Sulfoxide.Inactivation of thiol-dependent enzymes by hypothiocyanous acid: role of sulfenyl thiocyanate and sulfenic acid intermediates.Peroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity.RegB kinase activity is repressed by oxidative formation of cysteine sulfenic acid.An immunochemical approach to detect oxidized protein tyrosine phosphatases using a selective C-nucleophile tagReactivity, Selectivity, and Stability in Sulfenic Acid Detection: A Comparative Study of Nucleophilic and Electrophilic Probes.Persulfide reactivity in the detection of protein s-sulfhydration.Molecular Basis for Redox Activation of Epidermal Growth Factor Receptor KinaseExpanding the functional diversity of proteins through cysteine oxidation.Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies.Identification of critical ligand binding determinants in Mycobacterium tuberculosis adenosine-5'-phosphosulfate reductase.Chemical biology approaches to study protein cysteine sulfenylation.Functional Site Discovery in a Sulfur Metabolism Enzyme by Using Directed Evolution.Rational design of reversible and irreversible cysteine sulfenic acid-targeted linear C-nucleophiles.
P50
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P50
description
researcher ORCID ID = 0000-0002-7624-9617
@en
name
Kate Carroll
@ast
Kate Carroll
@en
Kate Carroll
@es
Kate Carroll
@nl
type
label
Kate Carroll
@ast
Kate Carroll
@en
Kate Carroll
@es
Kate Carroll
@nl
prefLabel
Kate Carroll
@ast
Kate Carroll
@en
Kate Carroll
@es
Kate Carroll
@nl
P106
P108
P21
P31
P496
0000-0002-7624-9617