Publications by authors named "Christopher S Murphy"

In a few short years, the Internet (in terms of the World Wide Web) has become a powerful informational resource for the original scientific literature pertaining to biological investigations using the laser scanning confocal microscope. However, there still remains an obvious void in the development of educational Web sites targeted at beginning students and novices in the field. Furthermore, many of the commercial aftermarket manufacturers (for example, those offering live-cell imaging chambers) have Web sites that are not adequately represented in published compilations, and are therefore somewhat difficult to locate.

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DNA replication in all eukaryotes follows a defined replication timing program, the molecular mechanism of which remains elusive. Using a Xenopus laevis egg extract replication system, we previously demonstrated that replication timing is established during early G1 phase of the cell cycle (timing decision point [TDP]), which is coincident with the repositioning and anchorage of chromatin in the newly formed nucleus. In this study, we use this same system to show that G2 phase chromatin lacks determinants of replication timing but maintains the overall spatial organization of chromatin domains, and we confirm this finding by genome-wide analysis of rereplication in vivo.

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1,2,3-Triazol-4-yl (triazolyl)-containing tetradentate ligand 1 undergoes fluorescence enhancement upon binding to zinc ion (Zn(2+)) in both organic (acetonitrile) and aqueous solutions. A 1:1 complex of 1 with a trigonal bipyramidal Zn(2+) was characterized by X-ray crystallography. The cyclic voltammogram (CV) of 1 suggests that an intramolecular photoinduced electron transfer (PET) process is thermodynamically feasible which would quench the fluorescence of the 2-anthryltriazolyl fluorophore.

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A fluorescent heteroditopic ligand useful in live-cell imaging studies responds to free zinc ion concentration over a range of six orders of magnitude in a buffered aqueous solution via dual-channel fluorescence.

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Objective: To describe female soldiers' predeployment gynecologic healthcare screening, common symptoms, and availability of gynecologic care during Operation Iraqi Freedom.

Methods: A questionnaire distributed to U.S.

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We found that photoconversion is fairly common among orange and red fluorescent proteins, as in a screen of 12 proteins, 8 exhibited photoconversion. Specifically, three red fluorescent proteins could be switched to a green state, and two orange variants could be photoconverted to a far-red state. The orange proteins are ideal for dual-probe highlighter applications, and they exhibited the most red-shifted excitation of all fluorescent proteins described to date.

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Photoconvertible fluorescent proteins are potential tools for investigating dynamic processes in living cells and for emerging super-resolution microscopy techniques. Unfortunately, most probes in this class are hampered by oligomerization, small photon budgets or poor photostability. Here we report an EosFP variant that functions well in a broad range of protein fusions for dynamic investigations, exhibits high photostability and preserves the approximately 10-nm localization precision of its parent.

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A vast colour palette of monomeric fluorescent proteins has been developed to investigate protein localization, motility and interactions. However, low brightness has remained a problem in far-red variants, which hampers multicolour labelling and whole-body imaging techniques. In the present paper, we report mKate2, a monomeric far-red fluorescent protein that is almost 3-fold brighter than the previously reported mKate and is 10-fold brighter than mPlum.

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