Robbin Cathleen Lomax PA-C
Physician Assistant
9500 EUCLID AVE # E19 CLEVELAND OH, 44195About
Robbin Lomax is a physician assistant practicing in CLEVELAND, OH. Robbin specializes in preventing and treating human illness and injury by providing a broad range of care under the supervision of a physician. A physician assistant's work can include physical exams, ordering and interpreting tests, performing procedures and prescribing medication. Often times, they can assist in surgery but the scope of practice can vary according to jurisdiction or health care setting.
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Expert Publications
Data provided by the National Library of Medicine- In vitro analysis of the interaction between the FinO protein and FinP antisense RNA of F-like conjugative plasmids.
- Comparison of proteins involved in pilus synthesis and mating pair stabilization from the related plasmids F and R100-1: insights into the mechanism of conjugation.
- The FinO repressor of bacterial conjugation contains two RNA binding regions.
- Mobilization of chimeric oriT plasmids by F and R100-1: role of relaxosome formation in defining plasmid specificity.
- Crystal structure of the bacterial conjugation repressor finO.
- A rapid screen for functional mutants of TraM, an autoregulatory protein required for F conjugation.
- F factor conjugation is a true type IV secretion system.
- Bacterial conjugation: everybody's doin' it.
- Differential levels of fertility inhibition among F-like plasmids are related to the cellular concentration of finO mRNA.
- FinOP repression of the F plasmid involves extension of the half-life of FinP antisense RNA by FinO.
- The TraM protein of the conjugative plasmid F binds to the origin of transfer of the F and ColE1 plasmids.
- Examination of the phosphate in conjugative F-like pili by use of electron spectroscopic imaging.
- Structure and function of conjugative pili: monoclonal antibodies as probes for structural variants of F pili.
- Characterization of the oriT region of the IncFV plasmid pED208.
- A PAS domain within F plasmid TraJ is critical for its function as a transcriptional activator.
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