Jennifer Kim
Clinical Assistant Professor, Medicine - Primary Care and Population Health
Clinical Focus
- Internal Medicine
Professional Education
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Board Certification: American Board of Internal Medicine, Internal Medicine (2020)
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Medical Education: Rutgers Robert Wood Johnson Medical School (2011) NJ
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Chief Resident, Tufts Medical Center, MA (2014)
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Residency: Tufts Medical Center Internal Medicine Residency (2014) MA
All Publications
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Attitudes on cost-effectiveness and equity: a cross-sectional study examining the viewpoints of medical professionals
BMJ OPEN
2017; 7 (7): e017251
Abstract
To determine the attitudes of physicians and trainees in regard to the roles of both cost-effectiveness and equity in clinical decision making.In this cross-sectional study, electronic surveys containing a hypothetical decision-making scenario were sent to medical professionals to select between two colon cancer screening tests for a population.Three Greater Boston academic medical institutions: Tufts University School of Medicine, Tufts Medical Centre and Lahey Hospital and Medical Centre.819 medical students, 497 residents-in-training and 671 practising physicians were contacted electronically using institutional and organisational directories.Stratified opinions of medical providers and trainee subgroups regarding cost-effectiveness and equity.A total of 881 respondents comprising 512 medical students, 133 medical residents-in-training and 236 practising physicians completed the survey (total response rate 44.3%). Thirty-six per cent of medical students, 44% of residents-in-training and 53% of practising physicians favoured the less effective and more equitable screening test. Residents-in-training (OR 1.49, CI 1.01 to 2.21; p=0.044) and practising physicians (OR 2.12, CI 1.54 to 2.92; p<0.001) were more likely to favour the equitable option compared with medical students. Moreover, female responders across all three cohorts favoured the more equitable screening test to a greater degree than did male responders (OR 1.70, CI 1.29 to 2.24; p<0.001).Cost-effectiveness analysis does not accurately reflect the importance that medical professionals place on equity. Among medical professionals, practising physicians appear to be more egalitarian than residents-in-training, while medical students appear to be most utilitarian and cost-effective. Meanwhile, female respondents in all three cohorts favoured the more equitable option to a greater degree than their male counterparts. Healthcare policies that trade off equity in favour of cost-effectiveness may be unacceptable to many medical professionals, especially practising physicians and women.
View details for DOI 10.1136/bmjopen-2017-017251
View details for Web of Science ID 000410203700222
View details for PubMedID 28765138
View details for PubMedCentralID PMC5642791
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Mammalian sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation
MOLECULAR AND CELLULAR BIOLOGY
2007; 27 (24): 8807–14
Abstract
Homologs of the Saccharomyces cerevisiae Sir2 protein, sirtuins, promote longevity in many organisms. Studies of the sirtuin SIRT3 have so far been limited to cell culture systems. Here, we investigate the localization and function of SIRT3 in vivo. We show that endogenous mouse SIRT3 is a soluble mitochondrial protein. To address the function and relevance of SIRT3 in the regulation of energy metabolism, we generated and phenotypically characterized SIRT3 knockout mice. SIRT3-deficient animals exhibit striking mitochondrial protein hyperacetylation, suggesting that SIRT3 is a major mitochondrial deacetylase. In contrast, no mitochondrial hyperacetylation was detectable in mice lacking the two other mitochondrial sirtuins, SIRT4 and SIRT5. Surprisingly, despite this biochemical phenotype, SIRT3-deficient mice are metabolically unremarkable under basal conditions and show normal adaptive thermogenesis, a process previously suggested to involve SIRT3. Overall, our results extend the recent finding of lysine acetylation of mitochondrial proteins and demonstrate that SIRT3 has evolved to control reversible lysine acetylation in this organelle.
View details for DOI 10.1128/MCB.01636-07
View details for Web of Science ID 000251527300033
View details for PubMedID 17923681
View details for PubMedCentralID PMC2169418