Publications by authors named "Sarah E Bergholtz"
Objectives: To characterize the role of pathology explanation clinics (PECs) in prostate cancer care and determine their impact on patients, urologic oncologists, and quality of care.
Methods: Semistructured interviews with 10 patients with newly diagnosed prostate cancer were conducted before and after a PEC pilot and at the 1- and 6-month follow-up visits. Information about participants' cancer knowledge and anxiety were collected quantitatively.
Objectives: To characterize the attitudes of treating clinicians toward pathology explanation clinics (PECs).
Methods: Clinicians from a tertiary care academic medical center were asked, "How interested would you be in having your patient meet with a pathologist to discuss their pathology report and see their tissue under the microscope?" Clinicians ranked their interest, then expanded on concerns and benefits in a semistructured interview. Audio recordings of interviews were transcribed and analyzed using a qualitative thematic approach.
Lysine malonylation is a recently characterized post-translational modification involved in the regulation of energy metabolism and gene expression. One unique feature of this post-translational modification is its potential susceptibility to decarboxylation, which poses possible challenges to its study. As a step towards addressing these challenges, we report the synthesis and evaluation of a stable isostere of malonyllysine.
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- HLRCC is a genetic cancer syndrome linked to mutations in the fumarate hydratase enzyme, leading to the accumulation of fumarate, which can alter gene activity and promote tumor formation.
- A chemoproteomic analysis of kidney-derived HLRCC cell lines revealed a significant change in cysteine reactivity when fumarate levels were reduced by reintroducing functional FH, indicating both transcriptional and posttranslational mechanisms at play.
- The study identified new targets and pathways affected by FH mutations and emphasized the diversity of protein responses in different HLRCC models, suggesting the need for further exploration of tissue-specific adaptations for potential cancer therapies.
Metabolites regulate protein function via covalent and noncovalent interactions. However, manipulating these interactions in living cells remains a major challenge. Here, we report a chemical strategy for inducing cysteine S-succination, a nonenzymatic post-translational modification derived from the oncometabolite fumarate.
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- Acyl-CoA/protein interactions are vital for biological functions, but their overall scope and selectivity are not yet fully understood.
- The study introduces CATNIP, a method for analyzing these interactions in a high-throughput manner, allowing researchers to identify acetyl-CoA-binding proteins and their selectivity.
- The research combines chemoproteomics and systems biology to explore acyl-CoA metabolism's implications in biology and disease, revealing significant insights such as a non-enzymatic acylation site in the NAT10 acetyltransferase domain.
Hereditary cancer disorders often provide an important window into novel mechanisms supporting tumor growth. Understanding these mechanisms thus represents a vital goal. Toward this goal, here we report a chemoproteomic map of fumarate, a covalent oncometabolite whose accumulation marks the genetic cancer syndrome hereditary leiomyomatosis and renal cell carcinoma (HLRCC).
View Article and Find Full Text PDFDysregulated metabolism can fuel cancer by altering the production of bioenergetic building blocks and directly stimulating oncogenic gene-expression programs. However, relatively few optical methods for the direct study of metabolites in cells exist. To address this need and facilitate new approaches to cancer treatment and diagnosis, herein we report an optimized chemical approach to detect the oncometabolite fumarate.
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