Aggregation deaggregation influenced selective and sensitive detection of Cu2+ and ATP by histidine functionalized water-soluble fluorescent perylene diimide under physiological conditions and in living cells

A novel PDI-HIS probe detects Cu2+ to form aggregated nonfluorescent complex. Addition of 0.58 ppm ATP to this complex causes its rapid disaggregation thereby recovering the fluorescence by ∼99% in vitro and in A549 living cells.

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Fluorescence turn-on for the highly selective detection of nitric oxide in vitro and in living cells

The Analyst ◽

10.1039/c6an00110f ◽

2016 ◽

Vol 141 (8) ◽

pp. 2600-2605 ◽

Cited By ~ 15

Author(s):

Xiaomei Liu ◽

Shuang Liu ◽

Gaolin Liang

Keyword(s):

Nitric Oxide ◽

Living Cells ◽

Water Soluble ◽

Sensitive Detection ◽

Selective Detection ◽

Turn On ◽

Fluorescence Turn On

A water-soluble, biocompatible, small molecular fluorescent turn-on probe was developed for the highly selective and sensitive detection of NO in vitro and in living cells.

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An efficient strategy to assemble water soluble histidine-perylene diimide and graphene oxide for the detection of PPi in physiological conditions and in vitro

Biosensors and Bioelectronics ◽

10.1016/j.bios.2015.12.036 ◽

2017 ◽

Vol 89 ◽

pp. 636-644 ◽

Cited By ~ 17

Author(s):

B. Muthuraj ◽

Sudip Mukherjee ◽

Sayan Roy Chowdhury ◽

Chitta Ranjan Patra ◽

Parameswar K. Iyer

Keyword(s):

Graphene Oxide ◽

Water Soluble ◽

Perylene Diimide ◽

Physiological Conditions ◽

Efficient Strategy

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Condensed chromatin behaves like a solid on the mesoscale in vitro and in living cells

10.1101/2020.05.06.079905 ◽

2020 ◽

Cited By ~ 2

Author(s):

Hilmar Strickfaden ◽

Thomas Tolsma ◽

Ajit Sharma ◽

D. Alan Underhill ◽

Jeffrey C. Hansen ◽

...

Keyword(s):

Nuclear Dna ◽

Living Cells ◽

Physiological Conditions ◽

Transmission Electron ◽

Material State ◽

Temporal And Spatial ◽

Self Association ◽

Eukaryotic Genomes

SUMMARYThe association of nuclear DNA with histones to form chromatin is essential to the temporal and spatial control of eukaryotic genomes. In this study, we examined the physical state of chromatin in vitro and in vivo. Our in vitro studies demonstrate that MgCl2-dependent self-association of native chromatin fragments or reconstituted nucleosomal arrays produced supramolecular condensates whose constituents are physically constrained and solid-like. Liquid chromatin condensates could be generated in vitro, but only using non-physiological conditions. By measuring DNA mobility within heterochromatin and euchromatin in living cells, we show that chromatin also exhibits solid-like behavior in vivo. Representative heterochromatin proteins, however, displayed liquid-like behavior and coalesced around a solid chromatin scaffold. Remarkably, both euchromatin and heterochromatin showed solid-like behavior even when transmission electron microscopy revealed limited interactions between chromatin fibers. Our results therefore argue that chromatin is not liquid but exists in a solid-like material state whose properties are tuned by fiber-fiber interactions.

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A Bio-Photonics System for Rapid In Vitro Testing of Cells and Ceramics

Key Engineering Materials ◽

10.4028/www.scientific.net/kem.284-286.531 ◽

2005 ◽

Vol 284-286 ◽

pp. 531-536 ◽

Cited By ~ 1

Author(s):

Larry L. Hench ◽

Ioan Notingher

Keyword(s):

Cell Damage ◽

Spectroscopic Method ◽

Living Cells ◽

In Vitro Cultures ◽

Animal Testing ◽

Time Analysis ◽

Cellular Functions ◽

Physiological Conditions ◽

Real Time Analysis

We present a new bio-photonic method based on Raman spectroscopy able to characterize living cells in in-vitro cultures. The main advantages of this technology are: no labels or other contrast enhancers are required; provides real-time analysis; cells can be maintained in physiological conditions during the measurements; no cell-damage is induced during the measurements; it is rich in information about the biochemical composition of the cell. The results show that this spectroscopic method can be used to study the most important cellular functions involved in cell-biomaterial interactions, such as cell death, differentiation, de-differentiation and mineralization. The method offers the potential for studying cell-bioceramics interaction and reduce the need of animal testing until the final steps of proving efficacy prior to clinical trials.

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Synthesis and anti-cancer activities of a water soluble gold(III) porphyrin

Journal of Porphyrins and Phthalocyanines ◽

10.1142/s1088424615500236 ◽

2015 ◽

Vol 19 (01-03) ◽

pp. 398-403 ◽

Cited By ~ 12

Author(s):

Aaron D. Lammer ◽

Melissa E. Cook ◽

Jonathan L. Sessler

Keyword(s):

Anticancer Agents ◽

Ovarian Cancer Cell ◽

Ovarian Cancer Cell Line ◽

Aqueous Media ◽

Cancer Cell Line ◽

Aqueous Solubility ◽

Water Soluble ◽

Physiological Conditions ◽

Anti Cancer

Gold(III) compounds continue to be explored for their potential utility as anticancer agents. A recognized limitation is the reactivity of gold(III), which is typically reduced to the more labile gold(I) state under physiological conditions. The use of porphyrins can overcome this problem. However, to date the stabilization provided by the use a strongly chelating porphyrin is offset by the poor solubility of the resulting complex in aqueous media. In this work, we describe the synthesis and in vitro anti-cancer activity of a gold(III)porphyrin complex with relatively good aqueous solubility. As judged from standard antiproliferation assays, this complex displays an IC50 of 9 μM for the A2780 human ovarian cancer cell line. This is a higher level of potency than displayed by two related control systems.

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Overlapping Functions of the pRb Family in the Regulation of rRNA Synthesis

Molecular and Cellular Biology ◽

10.1128/mcb.21.17.5806-5814.2001 ◽

2001 ◽

Vol 21 (17) ◽

pp. 5806-5814 ◽

Cited By ~ 49

Author(s):

Sonia Ciarmatori ◽

Pamela H. Scott ◽

Josephine E. Sutcliffe ◽

Angela McLees ◽

Hadi M. Alzuherri ◽

...

Keyword(s):

Living Cells ◽

Rrna Synthesis ◽

Pocket Proteins ◽

Physiological Conditions ◽

Pol I ◽

Binding Factor ◽

Upstream Binding Factor ◽

Negative Growth

ABSTRACT The “pocket” proteins pRb, p107, and p130 are a family of negative growth regulators. Previous studies have demonstrated that overexpression of pRb can repress transcription by RNA polymerase (Pol) I. To assess whether pRb performs this role under physiological conditions, we have examined pre-rRNA levels in cells from mice lacking either pRb alone or combinations of the three pocket proteins. Pol I transcription was unaffected in pRb-knockout fibroblasts, but specific disruption of the entire pRb family deregulated rRNA synthesis. Further analysis showed that p130 shares with pRb the ability to repress Pol I transcription, whereas p107 is ineffective in this system. Production of rRNA is abnormally elevated in Rb−/−p130−/− fibroblasts. Furthermore, overexpression of p130 can inhibit an rRNA promoter both in vitro and in vivo. This reflects an ability of p130 to bind and inactivate the upstream binding factor, UBF. The data imply that rRNA synthesis in living cells is subject to redundant control by endogenous pRb and p130.

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Association of fibronectin with carboxy-group-modified proteins in vitro

Biochemical Journal ◽

10.1042/bj2050303 ◽

1982 ◽

Vol 205 (2) ◽

pp. 303-311 ◽

Cited By ~ 3

Author(s):

Matti Vuento ◽

Mirja Korkolainen ◽

Ulf-Hȧkan Stenman

Keyword(s):

Carboxy Group ◽

Immunoglobulin G ◽

Reticuloendothelial System ◽

Water Soluble ◽

Heat Denaturation ◽

Ph Optimum ◽

Binding Reaction ◽

Physiological Conditions ◽

Modified Proteins

Treatment of human immunoglobulin G, albumin and fibronectin with water-soluble carbodi-imide at pH4.75 in the presence of glycine ethyl ester resulted in an avid binding of 125I-labelled native fibrinectin to the modified proteins. Succinoylation, reduction and alkylation or heat-denaturation had no such effect. In affinity chromatography under physiological conditions, serum was depleted of fibronectin when run through columns of the carbodi-imide-treated proteins coupled to agarose. Fractions eluted from such columns with urea were enriched in fibronectin. The binding of radiolabelled fibronectin to the carbodi-imide-treated proteins was inhibited by unlabelled fibronectin in relatively low concentrations, but also by albumin in higher concentrations. Heat-denatured albumin inhibited at concentrations approx. 10–30 times lower than native albumin. The binding reaction had a pH optimum of 6–8. It was inhibited at high ionic strength and in the presence of urea. Anionic detergents inhibited at millimolar concentrations, but non-ionic detergents did not inhibit the binding reaction. The results were interpreted as showing that: (1) fibronectin is capable of binding to itself, to immunoglobulin G and to albumin after a reduction of the negative surface charge of these proteins, and may have a general ability to bind such modified proteins; (2) this binding can take place under physiological conditions; (3) carboxy-group-modified proteins selectively bind fibronectin from serum. This novel binding phenomenon could be important in terms of the opsonin function of circulatory fibronectin. We propose that fibronectin may recognize modified (denatured) proteins and mediate their uptake by the reticuloendothelial system.

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