Family Practitioner
7 years of experience

Accepting new patients
Coronado Area
Grace Clinic Lubbock
4515 Marsha Sharp Fwy
Lubbock, TX 79407
806-744-7223
Locations and availability (1)

Education ?

Medical School Score Rankings
Baylor College of Medicine (2003)
  • Currently 4 of 4 apples
Top 25%
Residency
University Medical Center - Lubbock (2006) *
Family Medicine
* This information was reported to Vitals by the doctor or doctor's office.

Awards & Distinctions ?

Associations
American Board of Family Medicine

Affiliations ?

Dr. Crossnoe is affiliated with 8 hospitals.

Hospital Affilations

Score

Rankings

  • Covenant Medical Center
    3615 19th St, Lubbock, TX 79410
    • Currently 4 of 4 crosses
    Top 25%
  • Highland Medical Center
    2412 50th St, Lubbock, TX 79412
    • Currently 3 of 4 crosses
    Top 50%
  • University Medical Center - Lubbock *
    602 Indiana Ave, Lubbock, TX 79415
    • Currently 2 of 4 crosses
  • Covenant Hospital Levelland
    1900 College Ave, Levelland, TX 79336
    • Currently 2 of 4 crosses
  • Covenant Children's Hospital
    3610 21st St, Lubbock, TX 79410
    • Currently 2 of 4 crosses
  • Covenant Hospital Plainview
    2601 Dimmitt Rd, Plainview, TX 79072
    • Currently 1 of 4 crosses
  • University Medical Center
  • Grace Medical Center *
  • Publications & Research

    Dr. Crossnoe has contributed to 2 publications.
    Title Reactivity of Reduced [2fe-2s] Ferredoxins Parallels Host Susceptibility to Nitroimidazoles.
    Date June 2003
    Journal Antimicrobial Agents and Chemotherapy
    Excerpt

    The kinetics of the electron transfer reaction between reduced [2Fe-2S] ferredoxins and select nitroimidazole antimicrobial agents is reported. The ferredoxins from the protozoan Trichomonas vaginalis and the cyanobacterium Anabaena sp. strain 7120 were studied because they are the proximal electron donors to nitroimidazoles in these two organisms with significantly different nitroimidazole susceptibilities. The rates of electron transfer from Anabaena ferredoxin to all nitroimidazoles were 1 to 2 orders of magnitude lower than for T. vaginalis ferredoxin. Quantitative structure-activity analysis of the kinetic data showed that the size of the alkyl substituent on the N-1 position of the imidazole ring strongly influenced the magnitude of the electron transfer rate constant. This implies that the distance between the iron-sulfur cluster and the nitro group of the imidazole is the critical variable in determining the rate of electron transfer. A correlation between the magnitude of the one-electron transfer rate constant with the susceptibility of the host organism to the cytotoxic effects of nitroimidazoles was also discovered. These results demonstrate that reductive activation is the most crucial step in determining the toxicity of nitroimidazoles.

    Title The Crystal Structure of Trichomonas Vaginalis Ferredoxin Provides Insight into Metronidazole Activation.
    Date June 2002
    Journal Journal of Molecular Biology
    Excerpt

    Crystallographic studies revealing the three-dimensional structure of the oxidized form of the [2Fe-2S] ferredoxin from Trichomonas vaginalis (TvFd) are presented. TvFd, a member of the hydrogenosomal class of ferredoxins, possesses a unique combination of redox and spectroscopic properties, and is believed to be the biological molecule that activates the drug metronidazole reductively in the treatment of trichomoniasis. It is the first hydrogenosomal ferredoxin to have its structure determined. The structure of TvFd reveals a monomeric, 93 residue protein with a fold similar to that of other known [2Fe-2S] ferredoxins. It contains nine hydrogen bonds to the sulfur atoms of the cluster, which is more than the number predicted on the basis of the spectroscopic data. The TvFd structure contains a large dipole moment like adrenodoxin, and appears to have a similar interaction domain. Our analysis demonstrates that TvFd has a unique cavity near the iron-sulfur cluster that exposes one of the inorganic sulfur atoms of the cluster to solvent. This cavity is not seen in any other [2Fe-2S] ferredoxin with known structure, and is hypothesized to be responsible for the high rate of metronidazole reduction by TvFd.


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