C
Cristina M. Furdui
Researcher at Wake Forest University
Publications - 156
Citations - 4560
Cristina M. Furdui is an academic researcher from Wake Forest University. The author has contributed to research in topics: Medicine & Internal medicine. The author has an hindex of 31, co-authored 127 publications receiving 3411 citations. Previous affiliations of Cristina M. Furdui include University of Nebraska–Lincoln & Yale University.
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Effects of ionizing radiation on biological molecules--mechanisms of damage and emerging methods of detection.
TL;DR: Chemical mechanisms for IR-induced modifications of biomolecules along with methods for their detection are described and the synergy of combined "omics" technologies such as genomics and epigenomics, proteomics, and metabolomics is highlighted.
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Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction.
TL;DR: It is proposed that FGFR1 is activated by a two-step mechanism mediated by strictly ordered and regulated autophosphorylation, suggesting that distinct phosphorylation states may provide both temporal and spatial resolution to receptor signaling.
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Stearoyl-CoA Desaturase 1 Protects Ovarian Cancer Cells from Ferroptotic Cell Death.
Lia Tesfay,Bibbin T. Paul,Anna Konstorum,Zhiyong Deng,Anderson Cox,Jingyun Lee,Cristina M. Furdui,Poornima Hegde,Frank M. Torti,Suzy V. Torti +9 more
TL;DR: The results suggest that the use of combined treatment with SCD1 inhibitors and ferroptosis inducers may provide a new therapeutic strategy for patients with ovarian cancer, since overcoming this dual mechanism of cell death may present a significant barrier to the emergence of drug resistance.
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The role of pyruvate ferredoxin oxidoreductase in pyruvate synthesis during autotrophic growth by the Wood-Ljungdahl pathway
TL;DR: The results described here demonstrate that the Clostridium thermoaceticum PFOR is a highly efficient pyruvate synthase in vivo andMeasurements of itsk cat/K m values demonstrate that ferredoxin is ahighly efficient electron carrier in both the oxidative and reductive reactions.
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Fluorescent and affinity-based tools to detect cysteine sulfenic acid formation in proteins
Leslie B. Poole,Chananat Klomsiri,Sarah A. Knaggs,Cristina M. Furdui,Kimberly J. Nelson,Michael J. Thomas,Jacquelyn S. Fetrow,Larry W. Daniel,S. Bruce King +8 more
TL;DR: The arsenal of tagging reagents is expanded to include two fluorescein-, two rhodamine-, and three biotin-conjugated probes based on the original approach, which provide readily detectable fluorescent and affinity probes to identify sulfenic acid modifications in proteins and have been used in subsequent mass spectrometric analyses.