P
Polly M. Fordyce
Researcher at Stanford University
Publications - 95
Citations - 2518
Polly M. Fordyce is an academic researcher from Stanford University. The author has contributed to research in topics: Biology & Transcription factor. The author has an hindex of 19, co-authored 70 publications receiving 1953 citations. Previous affiliations of Polly M. Fordyce include University of California & University of California, San Francisco.
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Journal ArticleDOI
Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro.
TL;DR: It is found that the velocity of Eg5 was slower and less sensitive to external load than that of conventional kinesin, possibly reflecting the distinct demands of spindle assembly as compared with vesicle transport.
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Simultaneous, coincident optical trapping and single-molecule fluorescence.
TL;DR: A microscope-based instrument capable of simultaneous, spatially coincident optical trapping and single-molecule fluorescence is constructed and the distance to the thermodynamic transition state and the thermal off rates in the absence of load for both processes are determined.
Journal ArticleDOI
De novo identification and biophysical characterization of transcription-factor binding sites with microfluidic affinity analysis
Polly M. Fordyce,Polly M. Fordyce,Doron Gerber,Danh Tran,Jiashun Zheng,Hao Li,Hao Li,Joseph L. DeRisi,Joseph L. DeRisi,Stephen R. Quake,Stephen R. Quake +10 more
TL;DR: A microfluidics-based approach for de novo discovery and quantitative biophysical characterization of DNA target sequences, validated by measuring sequence preferences for 28 Saccharomyces cerevisiae transcription factors with a variety of DNA-binding domains, including several that have proven difficult to study by other techniques.
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Stepping and stretching. How kinesin uses internal strain to walk processively.
Steven S. Rosenfeld,Polly M. Fordyce,Geraldine M. Jefferson,Peter H. King,Peter H. King,Steven M. Block +5 more
TL;DR: The data argue that the major effect of the internal strain generated when both motor domains of kinesin bind the microtubule is to block ATP from binding to the leading motor, guaranteeing the two motor domains remain out of phase for many mechanochemical cycles and provides an efficient and adaptable mechanism for the maintenance of processive movement.
Journal ArticleDOI
Structure of the transcriptional network controlling white‐opaque switching in Candida albicans
Aaron D. Hernday,Matthew B. Lohse,Polly M. Fordyce,Polly M. Fordyce,Clarissa J. Nobile,Joseph L. DeRisi,Joseph L. DeRisi,Alexander D. Johnson +7 more
TL;DR: This work describes the structure of the transcriptional network that specifies the white and opaque cell types and governs the ability to switch between them and proposes that the structure (or topology) of this network is responsible for the epigenetic maintenance of thewhite and opaque states, the switching between them, and the specialized properties of each state.