William Edward Walden D.M.D.
Dentist
5154 Village Square Dr Paducah KY, 42001About
Dr. William Walden is a Dentist practicing in Paducah, KY. Dr. Walden specializes in preventing, diagnosing, and treating diseases and conditions associated with the mouth and overall dental health. Dentists are trained to carry out such treatment as professional cleaning, restorative, prosthodontic, and endodontic procedures, and performing examinations, among many others.
Provider Details
Expert Publications
Data provided by the National Library of Medicine- The aconitase function of iron regulatory protein 1. Genetic studies in yeast implicate its role in iron-mediated redox regulation.
- Detection of a [3Fe-4S] cluster intermediate of cytosolic aconitase in yeast expressing iron regulatory protein 1. Insights into the mechanism of Fe-S cluster cycling.
- From bacteria to mitochondria: aconitase yields surprises.
- Schizosaccharomyces pombe Ddb1 is functionally linked to the replication checkpoint pathway.
- A novel eukaryotic factor for cytosolic Fe-S cluster assembly.
- Cloning of a functional cDNA for the rabbit ferritin mRNA repressor protein. Demonstration of a tissue-specific pattern of expression.
- Crystallization and preliminary X-ray diffraction analysis of iron regulatory protein 1 in complex with ferritin IRE RNA.
- Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA.
- Characteristics of the interaction of the ferritin repressor protein with the iron-responsive element.
- Ferritin mRNA: interactions of iron regulatory element with translational regulator protein P-90 and the effect on base-paired flanking regions.
- Direct Fe2+ sensing by iron-responsive messenger RNA:repressor complexes weakens binding.
- Cytosolic iron-sulfur cluster assembly (CIA) system: factors, mechanism, and
- Crosslinking of hemin to a specific site on the 90-kDa ferritin repressor protein.
- Induction of ferritin synthesis in vitro: problems of specificity inherent in the use of iron compounds.
- Specificity of the induction of ferritin synthesis by hemin.
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