Today's Hours: 12:00pm - 8:00pm
Lane Medical Library

Search

Filter Results

Did You Mean:

Search Results

Sort by
relevance
  • Book
    Michelle Kittleson.
    Summary: Like a mentor you may turn to in times of crisis, this book provides the wisdom earned from countless mentors and patients. You may be standing on the precipice of medical training or well into your career, trying to recapture the joy of medicine. A love of people and a love of science barely capture the essence of a life in medicine; there is so much more to being a physician than the ability to diagnose and treat diseases. While nothing can fully prepare you for the fear and anxiety that comes with inexperience, Mastering the Art of Patient Care eases some of that uncertainty with a system for surviving and thriving in medical school and beyond. Whatever your stage, the goal of this book is to share successes and failures to help you be a physician who takes outstanding care of patients, colleagues, and trainees and derives great joy from saving lives.

    Contents:
    Medical School
    Becoming Fluent in Medicine
    Your Career Path
    Diagnosis
    Tests and Interventions
    The Art of the Consult
    Good Habits for a Lifetime
    Leading Your Team
    The Tough Conversations
    The Patient-Physician Bond
    Being a Woman in Medicine
    Self-care
    What Covid Has Taught Us (or Not)
    The Joy of Medicine.
    Digital Access Springer 2022
  • Article
    VanDerLijn P, Barrio JR, Leonard NJ.
    J Biol Chem. 1978 Dec 25;253(24):8694-6.
    The interaction of Escherichia coli aspartate transcarbamylase with linear-benzo-ATP has been investigated by means of fluorescence spectroscopy. The fluorescent nucleotide analogue activates the enzyme to the same extent as ATP. Fluorescence polarization has been used to determine the association constant of lin-benzo-ATP with aspartate transcarbamylase (ATCase) which is 5 X 10(-3) M-1 at pH 8.7, at 4 degrees C, assuming six binding sites. This association constant is similar to those previously obtained for ATP at a variety of temperatures, buffers, and pH. The fluorescence emission of lin-benzo-ATP is not quenched when bound to ATCase, which indicates absence of pi interactions between the activator and tyrosyl residues in the protein. These residues have been implicated in the stereochemical mechanism of allosteric interactions in ATCase. Furthermore, this fluorescence behavior implicates hydrogen bond formation between the amino group of lin-benzo-ATP and a nucleophilic center at the enzyme binding site. The fact that lin-benzo-ATP activates ATCase is consistent with a previously published model for nucleotide regulation of the enzyme.
    Digital Access Access Options
  • Journal
    Print Jan. 1926-1970.