Karen S. Conrad

ORCID: 0000-0003-3048-2226
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About
Contact & Profiles
Research Areas
  • Light effects on plants
  • Folate and B Vitamins Research
  • Porphyrin Metabolism and Disorders
  • Photosynthetic Processes and Mechanisms
  • Heme Oxygenase-1 and Carbon Monoxide
  • Lysosomal Storage Disorders Research
  • Photoreceptor and optogenetics research
  • Cellular transport and secretion
  • Calcium signaling and nucleotide metabolism
  • Methane Hydrates and Related Phenomena
  • Microbial Metabolic Engineering and Bioproduction
  • Geological Studies and Exploration
  • bioluminescence and chemiluminescence research
  • Education, Achievement, and Giftedness
  • Iron Metabolism and Disorders
  • Plant and Biological Electrophysiology Studies
  • Cognitive and developmental aspects of mathematical skills
  • School Choice and Performance

Pfizer (United States)
2017

Cornell University
2012-2016

University of Wisconsin–Madison
2008-2015

Light–oxygen–voltage (LOV) domains bind a flavin chromophore to serve as blue light sensors in wide range of eukaryotic and prokaryotic proteins. LOV are associated with variable effector domain or separate protein signaling partner execute variety functions that include regulation kinases, generation anti-sigma factor antagonists, circadian clocks. Here we present the crystal structure, photocycle kinetics, association properties, spectroscopic features full-length from Rhodobacter...

10.1021/bi3015373 article EN Biochemistry 2012-12-19

Lysosomal integral membrane protein-2 (LIMP-2/SCARB2) contributes to endosomal and lysosomal function. LIMP-2 deficiency is associated with neurological abnormalities kidney failure and, as an acid glucocerebrosidase receptor, impacts Gaucher Parkinson's diseases. Here we report a crystal structure of luminal domain dimer bound cholesterol phosphatidylcholine. Binding these lipids alters from functioning glucocerebrosidase-binding monomer toward dimeric state that preferentially binds...

10.1038/s41467-017-02044-8 article EN cc-by Nature Communications 2017-11-28

Glutathionylcobalamin (GSCbl) is a unique, biologically relevant cobalamin featuring an axial Co–S bond that distinguishes it from the enzymatically active forms of vitamin B12, which possess Co–C bonds. GSCbl has been proposed to serve as intermediate in processing and, more recently, therapeutic for neurological disorders associated with oxidative stress. In this study, and its close relative cysteinylcobalamin (CysCbl) were investigated using electronic absorption, circular dichroism,...

10.1021/ic200428r article EN Inorganic Chemistry 2011-08-22

Vitamin B12 (cyanocobalamin) and its biologically active derivatives, methylcobalamin adenosylcobalamin, are members of the family corrinoids, which also includes cobinamides. As biological precursors to cobalamins, cobinamides possess same structural core, consisting a low-spin Co3+ ion that is ligated equatorially by four nitrogens highly substituted tetrapyrrole macrocycle (the corrin ring), but differ with respect lower axial ligation. Specifically, water molecule instead nucleotide loop...

10.1021/ic202052g article EN Inorganic Chemistry 2012-02-14

5′-deoxyadenosylcobalamin (coenzyme B12, AdoCbl) serves as the cofactor for several enzymes that play important roles in fermentation and catabolism. All of these initiate catalysis by promoting homolytic cleavage cofactor's Co–C bond response to substrate binding their active sites. Despite considerable research efforts, role lower axial ligand facilitating homolysis remains incompletely understood. In present study, we characterized derivatives AdoCbl its one-electron reduced form,...

10.1021/ic502665x article EN Inorganic Chemistry 2015-04-03
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