S
Sanford H. Leuba
Researcher at University of Pittsburgh
Publications - 64
Citations - 3094
Sanford H. Leuba is an academic researcher from University of Pittsburgh. The author has contributed to research in topics: Chromatin & Histone. The author has an hindex of 31, co-authored 64 publications receiving 3005 citations. Previous affiliations of Sanford H. Leuba include University of Wyoming & University of Oregon.
Papers
More filters
Journal ArticleDOI
Single molecule force spectroscopy in biology using the atomic force microscope
TL;DR: This review focuses on force measurements performed with the atomic force microscope, with a general introduction to the principle of action and review of the types of interactions being studied, describing the main results and discussing the biological implications.
Journal ArticleDOI
Unfolding individual nucleosomes by stretching single chromatin fibers with optical tweezers.
TL;DR: Repeated stretching and relaxing of the fiber in the absence of egg extract showed that the loss of histone octamers was irreversible, comparable to forces reported for RNA- and DNA-polymerases.
Journal ArticleDOI
Three-dimensional structure of extended chromatin fibers as revealed by tapping-mode scanning force microscopy
Sanford H. Leuba,Guoliang Yang,Charles H. Robert,Bruno Samorì,K. E. Van Holde,Jordanka Zlatanova,Carlos Bustamante +6 more
TL;DR: The results, when compared with modeling studies, suggest that chromatin fibers may exist as irregular three-dimensional arrays of nucleosomes even at low ionic strength.
Journal ArticleDOI
Fast, long-range, reversible conformational fluctuations in nucleosomes revealed by single-pair fluorescence resonance energy transfer.
TL;DR: By single-pair fluorescence resonance energy transfer, this work demonstrates fast, long-range, reversible conformational fluctuations in nucleosomes between two states: fully folded (closed), with the DNA wrapped around the histone core, or open, with theDNA significantly unraveled from the hist one octamer.
Journal ArticleDOI
Proteins that specifically recognize cisplatin-damaged DNA: a clue to anticancer activity of cisplatin
TL;DR: Two classes of proteins have recently been identified that bind preferentially to damaged sites: proteins that specifically recognize those sites as a first step in their repair, and those that bind to such sites by virtue of structural similarity between the modified DNA and their own natural binding sites.