Dr. Michael R Nichols D.M.D., M.D.
Oral and Maxillofacial Surgeon | Oral and Maxillofacial Surgery
266 Katherine Dr Flowood MS, 39232About
Dr. Michael Nichols is an oral and maxillofacial surgeon practicing in Flowood, MS. Dr. Nichols specializes in the treatment of problems related to the face, mouth and jaws. As an oral and maxillofacial surgeon, Dr. Nichols is a unique dental specialist who can provide emergency medicine, perform general surgery and give anesthesia. These medical doctors are the only type of medical care specialist who can administer anesthesia, besides anesthesiologists. Typical procedures performed by Dr. Nichols are tooth extractions, especially wisdom teeth, corrective jaw surgery, cleft palate surgery and reconstructive surgery after an injury. Oral and maxillofacial surgeons can also perform dental work including placing dental implants. These surgeons might also deal with conditions of sleep apnea, oral cancers and more.
Education and Training
University of Mississippi School of Medicine 2000
University of Alabama School of Medicine 1998
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Growth of beta-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy.
- The peptide KLVFF-K(6) promotes beta-amyloid(1-40) protofibril growth by association but does not alter protofibril effects on cellular reduction of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT).
- Nordihydroguaiaretic acid does not disaggregate beta-amyloid(1-40) protofibrils but does inhibit growth arising from direct protofibril association.
- Amyloid-beta protofibrils differ from amyloid-beta aggregates induced in dilute hexafluoroisopropanol in stability and morphology.
- Rapid assembly of amyloid-beta peptide at a liquid/liquid interface produces unstable beta-sheet fibers.
- Amyloid-beta aggregates formed at polar-nonpolar interfaces differ from amyloid-beta protofibrils produced in aqueous buffers.
- Toll-like receptors 2 and 4 mediate Abeta(1-42) activation of the innate immune response in a human monocytic cell line.
- Oligomeric amyloid-beta(1-42) induces THP-1 human monocyte adhesion and maturation.
- Amyloid-beta(1-42) fibrillar precursors are optimal for inducing tumor necrosis factor-alpha production in the THP-1 human monocytic cell line.
- Probing the amyloid-beta(1-40) fibril environment with substituted tryptophan residues.
- Substituted tryptophans at amyloid-β(1-40) residues 19 and 20 experience different environments after fibril formation.
- Isolated amyloid-β(1-42) protofibrils, but not isolated fibrils, are robust stimulators of microglia.
- Stability of early-stage amyloid-beta(1-42) aggregation species.
- Amyloid-β(1-42) protofibrils formed in modified artificial cerebrospinal fluid bind and activate microglia.
- Amyloid-β(1-42) protofibrils stimulate a quantum of secreted IL-1β despite significant intracellular IL-1β accumulation in microglia.
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