Pages that link to "Q27659264"
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The following pages link to Structure of a bacterial homologue of vitamin K epoxide reductase (Q27659264):
Displayed 50 items.
- Human vitamin K 2,3-epoxide reductase complex subunit 1-like 1 (VKORC1L1) mediates vitamin K-dependent intracellular antioxidant function (Q24294610) (← links)
- Novel insight into the mechanism of the vitamin K oxidoreductase (VKOR): electron relay through Cys43 and Cys51 reduces VKOR to allow vitamin K reduction and facilitation of vitamin K-dependent protein carboxylation (Q24304387) (← links)
- Conserved loop cysteines of vitamin K epoxide reductase complex subunit 1-like 1 (VKORC1L1) are involved in its active site regeneration (Q24337424) (← links)
- Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria (Q26773784) (← links)
- Structural Modeling Insights into Human VKORC1 Phenotypes (Q26796613) (← links)
- VKORC1 and VKORC1L1: Why do Vertebrates Have Two Vitamin K 2,3-Epoxide Reductases? (Q26799185) (← links)
- Disulfide bond formation in the bacterial periplasm: major achievements and challenges ahead (Q26823827) (← links)
- Oxidative protein folding: selective pressure for prolamin evolution in rice (Q26824980) (← links)
- High-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental data (Q27674386) (← links)
- Structure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid Bilayer (Q27676407) (← links)
- Structure analysis of the extracellular domain reveals disulfide bond forming-protein properties of Mycobacterium tuberculosis Rv2969c (Q27678934) (← links)
- Rv2969c, essential for optimal growth inMycobacterium tuberculosis, is a DsbA-like enzyme that interacts with VKOR-derived peptides and has atypical features of DsbA-like disulfide oxidases (Q27680167) (← links)
- Structural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosis (Q27680391) (← links)
- Structures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transfer (Q27681521) (← links)
- Enzyme structure captures four cysteines aligned for disulfide relay (Q27684038) (← links)
- Cellular disulfide bond formation in bioactive peptides and proteins (Q28080871) (← links)
- Structural and functional insights into enzymes of the vitamin K cycle (Q28086880) (← links)
- The vitamin K oxidoreductase is a multimer that efficiently reduces vitamin K epoxide to hydroquinone to allow vitamin K-dependent protein carboxylation (Q28115117) (← links)
- Depletion of cyclophilins B and C leads to dysregulation of endoplasmic reticulum redox homeostasis (Q28243241) (← links)
- Disulfide bonds in ER protein folding and homeostasis (Q28300205) (← links)
- Structural basis for catalysis at the membrane-water interface. (Q30152692) (← links)
- Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems. (Q30376017) (← links)
- New pieces to an old puzzle: identifying the warfarin-binding site that prevents clotting (Q33364524) (← links)
- Electron Transport Chain Is Biochemically Linked to Pilus Assembly Required for Polymicrobial Interactions and Biofilm Formation in the Gram-Positive Actinobacterium Actinomyces oris (Q33820093) (← links)
- Genotype-based dosing algorithms for warfarin therapy: data review and recommendations (Q34065133) (← links)
- Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners (Q34093937) (← links)
- Evolutionary biochemistry: revealing the historical and physical causes of protein properties. (Q34358160) (← links)
- Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin (Q34519184) (← links)
- Coumatetralyl resistance of Rattus tanezumi infesting oil palm plantations in Indonesia (Q34522122) (← links)
- Membrane topology and mutational analysis of Mycobacterium tuberculosis VKOR, a protein involved in disulfide bond formation and a homologue of human vitamin K epoxide reductase (Q34700221) (← links)
- A hetero-dimer model for concerted action of vitamin K carboxylase and vitamin K reductase in vitamin K cycle. (Q35025482) (← links)
- Compounds targeting disulfide bond forming enzyme DsbB of Gram-negative bacteria (Q35196256) (← links)
- Mycobacterium tuberculosis vitamin K epoxide reductase homologue supports vitamin K-dependent carboxylation in mammalian cells (Q35635177) (← links)
- Food Reformulation, Responsive Regulation, and "Regulatory Scaffolding": Strengthening Performance of Salt Reduction Programs in Australia and the United Kingdom (Q35894964) (← links)
- Functional and evolutionary analyses of Helicobacter pylori HP0231 (DsbK) protein with strong oxidative and chaperone activity characterized by a highly diverged dimerization domain (Q36133918) (← links)
- Human vitamin K epoxide reductase and its bacterial homologue have different membrane topologies and reaction mechanisms (Q36298281) (← links)
- Altered Escherichia coli membrane protein assembly machinery allows proper membrane assembly of eukaryotic protein vitamin K epoxide reductase. (Q36371403) (← links)
- Evaluation of warfarin resistance using transcription activator-like effector nucleases-mediated vitamin K epoxide reductase knockout HEK293 cells (Q37100171) (← links)
- Oxidative protein-folding systems in plant cells (Q37239824) (← links)
- Operation of trans-thylakoid thiol-metabolizing pathways in photosynthesis (Q37346533) (← links)
- Integrating protein homeostasis strategies in prokaryotes (Q37858328) (← links)
- Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals. (Q38001127) (← links)
- The oxidative protein folding machinery in plant cells (Q38054482) (← links)
- Structural and functional insights into human vitamin K epoxide reductase and vitamin K epoxide reductase-like1. (Q38103055) (← links)
- Oxidative folding: recent developments (Q38472604) (← links)
- Antivitamins for Medicinal Applications (Q38503308) (← links)
- Functional Study of the Vitamin K Cycle Enzymes in Live Cells (Q39074534) (← links)
- The conservative cysteines in transmembrane domain of AtVKOR/LTO1 are critical for photosynthetic growth and photosystem II activity in Arabidopsis (Q39730215) (← links)
- Phylogeny of the Vitamin K 2,3-Epoxide Reductase (VKOR) Family and Evolutionary Relationship to the Disulfide Bond Formation Protein B (DsbB) Family (Q40673326) (← links)
- Warfarin traps human vitamin K epoxide reductase in an intermediate state during electron transfer. (Q41168727) (← links)