The use of botulinum toxin in the treatment of a parotid duct injury during Mohs surgery and review of management options.

Background: Aggressive skin cancers on the cheeks may involve the parotid duct. For such tumors to be successfully removed, at least part of the parotid duct must be excised as well. Failure to properly address parotid duct injuries that result from Mohs micrographic surgery exposes the patient to a variety of adverse sequelae.

Two-Carbon Compounds and Fatty Acids as Carbon Sources.

This review concerns the uptake and degradation of those molecules that are wholly or largely converted to acetyl-coenzyme A (CoA) in the first stage of metabolism in Escherichia coli and Salmonella enterica. These include acetate, acetoacetate, butyrate and longer fatty acids in wild type cells plus ethanol and some longer alcohols in certain mutant strains. Entering metabolism as acetyl-CoA has two important general consequences.

Fermentative Pyruvate and Acetyl-Coenzyme A Metabolism.

Pyruvate and acetyl-CoA form the backbone of central metabolism. The nonoxidative cleavage of pyruvate to acetyl-CoA and formate by the glycyl radical enzyme pyruvate formate lyase is one of the signature reactions of mixed-acid fermentation in enterobacteria. Under these conditions, formic acid accounts for up to one-third of the carbon derived from glucose.

Aesthetics and reconstruction--seeing before cutting.

In order to restore a specific form during aesthetic surgery it is self-evident that the surgeon needs to know the form exists. But more than this simple form restoration, the development of aesthetic restoration suggests a specific restoration in the context of the whole form. Developing a disciplined method of visualizing the problem is the first step toward being able to start an aesthetic sense or eye.

Regional variation in wound contraction of mohs surgery defects allowed to heal by second intention.

Background: The phenomenon of wound contraction results in a decrease in wound size and a healed scar significantly smaller than the original defect.

Objective: This study was undertaken (1) to determine the amount of wound contraction in Mohs surgery defects allowed to heal by second intention, (2) to evaluate for regional differences in wound contraction based on the facial anatomic zones for second intention healing described by Zitelli, and (3) to determine whether regional differences in wound contraction account for observed differences in cosmetic outcome.

Methods: One hundred sixty secondarily healed Mohs surgery defects limited to the head and neck having a wound age of greater than 12 weeks in 102 consecutively examined patients were carefully measured with a tissue caliper.

Structure-based mutagenesis approaches toward expanding the substrate specificity of D-2-deoxyribose-5-phosphate aldolase.

2-Deoxyribose-5-phosphate aldolase (DERA, EC 4.1.2.

Extensive overproduction of the AdhE protein by rng mutations depends on mutations in the cra gene or in the Cra-box of the adhE promoter.

Escherichia coli RNase G encoded by the rng gene is involved in degradation of adhE mRNA. Overproduction of the AdhE protein by rng mutants was found to depend on the genetic background of strains derived from DC272 (adhC81) or MC1061. We found that DC272 carried a point mutation in the Cra-binding site of the adhE promoter.

Identification of a CysB-regulated gene involved in glutathione transport in Escherichia coli.

Growth of Escherichia coli using the tripeptide glutathione as a sulfur source is well documented, but transport of glutathione into E. coli is uncharacterized. We have found that the ybiK gene, at 18.

Regulation of the ldhA gene, encoding the fermentative lactate dehydrogenase of Escherichia coli.

The fermentative lactate dehydrogenase (LDH) of Escherichia coli is induced by low pH under anaerobic conditions. Both translational and transcriptional gene fusions to ldhA, which encodes the fermentative LDH, have now been made. Both types of ldhA-lacZ fusion were induced by low pH, but only in the absence of air.

The ldhA gene encoding the fermentative lactate dehydrogenase of Escherichia coli.

Under anaerobic conditions, especially at low pH, Escherichia coli converts pyruvate to D-lactate by means of an NADH-linked lactate dehydrogenase (LDH). This LDH is present in substantial basal levels under all conditions but increases approximately 10-fold at low pH. The ldhA gene, encoding the fermentative lactate dehydrogenase of E.