Noninvasive, quantitative fluorescence sensing in 3D tissues: an approach to in vivo molecular characterization of engineered tissue constructs

2006 ◽  
Author(s):  
Malavika Chandra ◽  
Karthik Vishwanath ◽  
Greg D. Fichter ◽  
Elly Liao ◽  
Michael R. Francis ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Fluorescence Sensing ◽  
Tissue Constructs ◽  
Engineered Tissue ◽  
Quantitative Fluorescence

scholarly journals Molecular Characterization of HOXA2 and HOXA3 Binding Properties

2021 ◽  
Vol 9 (4) ◽  
pp. 55
Author(s):  
Joshua Mallen ◽  
Manisha Kalsan ◽  
Peyman Zarrineh ◽  
Laure Bridoux ◽  
Shandar Ahmad ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Molecular Characterization ◽  
Sequence Motif ◽  
Body Parts ◽  
Binding Affinities ◽  
Binding Properties ◽  
Functional Consequences

The highly conserved HOX homeodomain (HD) transcription factors (TFs) establish the identity of different body parts along the antero–posterior axis of bilaterian animals. Segment diversification and the morphogenesis of different structures is achieved by generating precise patterns of HOX expression along the antero–posterior axis and by the ability of different HOX TFs to instruct unique and specific transcriptional programs. However, HOX binding properties in vitro, characterised by the recognition of similar AT-rich binding sequences, do not account for the ability of different HOX to instruct segment-specific transcriptional programs. To address this problem, we previously compared HOXA2 and HOXA3 binding in vivo. Here, we explore if sequence motif enrichments observed in vivo are explained by binding affinities in vitro. Unexpectedly, we found that the highest enriched motif in HOXA2 peaks was not recognised by HOXA2 in vitro, highlighting the importance of investigating HOX binding in its physiological context. We also report the ability of HOXA2 and HOXA3 to heterodimerise, which may have functional consequences for the HOX patterning function in vivo.

Molecular characterization of the in vivo alkylating agent resistant murine EMT-6 mammary carcinoma tumors

1995 ◽  
Vol 35 (5) ◽  
pp. 423-431 ◽  
Author(s):  
Devasis Chatterjee ◽  
Chou Jui-Tsai Liu ◽  
David Northey ◽  
Beverly A. Teicher
Keyword(s):  
Molecular Characterization ◽  
Mammary Carcinoma ◽  
Alkylating Agent

scholarly journals Molecular characterization of the grape seeds extract’s effect against chemically induced liver cancer: In vivo and in vitro analyses

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Alaaeldin Ahmed Hamza ◽  
Gehan Hussein Heeba ◽  
Hanan Mohamed Elwy ◽  
Chandraprabha Murali ◽  
Raafat El-Awady ◽  
...  
Keyword(s):  
Liver Cancer ◽  
Molecular Characterization ◽  
Grape Seeds ◽  
Chemically Induced

Molecular characterization of the in vivo effects of the hemorrhagic metalloproteinase HF3: analysis of the proteome of mice muscle tissue

Toxicon ◽  
2019 ◽  
Vol 168 ◽  
pp. S21
Author(s):  
Eric Junqueira Brito Pereira ◽  
Dilza Trevisan Silva ◽  
Solange Maria De Toledo Serrano
Keyword(s):  
Molecular Characterization ◽  
Muscle Tissue ◽  
In Vivo Effects

scholarly journals Molecular characterization of centerin, a germinal centre cell serpin

2007 ◽  
Vol 405 (3) ◽  
pp. 489-494 ◽  
Author(s):  
Melinda A. Paterson ◽  
Anita J. Horvath ◽  
Robert N. Pike ◽  
Paul B. Coughlin
Keyword(s):  
B Cell ◽  
Serine Protease ◽  
Molecular Characterization ◽  
Good Prognosis ◽  
Germinal Centre ◽  
Lymphoid Malignancies ◽  
B Cell Maturation ◽  
Absolute Requirement

Centerin [SERPINA9/GCET1 (germinal centre B-cell-expressed transcript 1)] is a serpin (serine protease inhibitor) whose expression is restricted to germinal centre B-cells and lymphoid malignancies with germinal centre B-cell maturation. Expression of centerin, together with bcl-6 and GCET2, constitutes a germinal centre B-cell signature, which is associated with a good prognosis in diffuse large B-cell lymphomas, but the molecular basis for this remains to be elucidated. We report here the cloning, expression and molecular characterization of bacterial recombinant centerin. Biophysical studies demonstrated that centerin was able to undergo the ‘stressed to relaxed’ conformational change which is an absolute requirement for protease inhibitory activity. Kinetic analysis showed that centerin rapidly inhibited the serine protease trypsin (ka=1.9×105 M−1·s−1) and also demonstrated measurable inhibition of thrombin (ka=1.17×103 M−1·s−1) and plasmin (ka=1.92×103 M−1·s−1). Centerin also bound DNA and unfractionated heparin, although there was no functionally significant impact on the rate of inhibition. These results suggest that centerin is likely to function in vivo in the germinal centre as an efficient inhibitor of a trypsin-like protease.

scholarly journals Molecular characterization of precise in vivo targeted gene integration in human cells using AAVHSC15

PLoS ONE ◽  
2020 ◽  
Vol 15 (5) ◽  
pp. e0233373
Author(s):  
Huei-Mei Chen ◽  
Rachel Resendes ◽  
Azita Ghodssi ◽  
Danielle Sookiasian ◽  
Michael Tian ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Human Cells ◽  
Gene Integration ◽  
Targeted Gene Integration

scholarly journals In vivo phenotypic and molecular characterization of retinal degeneration in mouse models of three ciliopathies

2019 ◽  
Vol 186 ◽  
pp. 107721 ◽  
Author(s):  
Agnès Brun ◽  
Xiangxiang Yu ◽  
Cathy Obringer ◽  
Daniel Ajoy ◽  
Elodie Haser ◽  
...  
Keyword(s):  
Retinal Degeneration ◽  
Molecular Characterization ◽  
Mouse Models

Molecular Characterization of Gene Expression Changes in ROS 17/2.8 Cells Cultured in Diffusion Chambers In Vivo

1999 ◽  
Vol 65 (2) ◽  
pp. 133-138 ◽  
Author(s):  
J. E. Onyia ◽  
L. V. Hale ◽  
R. R. Miles ◽  
R. L. Cain ◽  
Y. Tu ◽  
...  
Keyword(s):  
Gene Expression ◽  
Molecular Characterization ◽  
Diffusion Chambers ◽  
Cells Cultured
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