Erratum: Rapid automated synthesis via diisopropyl phosphoramidite in situ activation. Chemical synthesis and cloning of a calmodulin gene

1986 ◽  
Vol 64 (12) ◽  
pp. 1382-1382
Author(s):  
G. Alvarado-Urbina ◽  
R. Chiarello ◽  
D. Roberts ◽  
G. Vilain ◽  
F. Jurik ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Automated Synthesis ◽  
Calmodulin Gene ◽  
In Situ Activation

Rapid automated synthesis via diisopropyl phosphoramidite in situ activation. Chemical synthesis and cloning of a calmodulin gene

1986 ◽  
Vol 64 (6) ◽  
pp. 548-555 ◽  
Author(s):  
G. Alvarado-Urbina ◽  
R. Chiarello ◽  
D. Roberts ◽  
G. Vilain ◽  
F. Jurik ◽  
...  
Keyword(s):  
Amino Acids ◽  
Chemical Synthesis ◽  
Solid Support ◽  
Automated Synthesis ◽  
Dna Fragments ◽  
Cleavage Sites ◽  
Gene Coding ◽  
In Situ Activation ◽  
Restriction Endonuclease Cleavage

A gene coding for a calmodulin was synthesized and cloned. The chemical synthesis of the gene, coding for 149 amino acids, was achieved by the enzymatic ligation of 61 chemically synthesized DNA fragments. The DNA fragments were synthesized using a solid support with a diisopropyl phosphoramidite intermediate and in situ activation. The automated standard cycle time was 10 min/addition. The synthesizer was designed and constructed from inexpensive, readily available parts and controlled by a Commodore 64 computer. The gene possesses 27 unique, regularly spaced, restriction endonuclease cleavage sites to facilitate gene mutagenesis.

A Photoactivatable α5β1-Specific Integrin Ligand

2018 ◽  
Author(s):  
Roshna Vakkeel ◽  
Aleeza Farrukh ◽  
Aranzazu del Campo
Keyword(s):  
Cellular Response ◽  
Light Exposure ◽  
Matrix Composition ◽  
Cellular Behavior ◽  
Dynamic Variations ◽  
In Situ Activation ◽  
Controlled Exposure ◽  
Cellular Behaviour ◽  
Integrin Ligand

In order to study how dynamic changes of α5β1 integrin engagement affect cellular behaviour, photoactivatable derivatives of α5β1 specific ligands are presented in this article. The presence of the photoremovable protecting group (PRPG) introduced at a relevant position for integrin recognition, temporally inhibits ligand bioactivity. Light exposure at cell-compatible dose efficiently cleaves the PRPG and restores functionality. Selective cell response (attachment, spreading, migration) to the activated ligand on the surface is achieved upon controlled exposure. Spatial and temporal control of the cellular response is demonstrated, including the possibility to in situ activation. Photoactivatable integrin-selective ligands in model microenvironments will allow the study of cellular behavior in response to changes in the activation of individual integrins as consequence of dynamic variations of matrix composition.

Comparative study of MoS2 and Co/MoS2 catalysts prepared by ex situ/in situ activation of ammonium and tetraalkylammonium thiomolybdates

2004 ◽  
Vol 210 (1-2) ◽  
pp. 105-117 ◽  
Author(s):  
L. Alvarez ◽  
J. Espino ◽  
C. Ornelas ◽  
J.L. Rico ◽  
M.T. Cortez ◽  
...  
Keyword(s):  
Comparative Study ◽  
Ex Situ ◽  
In Situ Activation ◽  
Mos2 Catalysts

Probing Structure Modification of Palladium Nanomaterials during Chemical Synthesis by using In Situ X-ray Diffraction: Electrochemical Properties

2015 ◽  
Vol 2 (4) ◽  
pp. 592-599 ◽  
Author(s):  
Yaovi Holade ◽  
Teko W. Napporn ◽  
Claudia Morais ◽  
Karine Servat ◽  
K. Boniface Kokoh
Keyword(s):  
Chemical Synthesis ◽  
Electrochemical Properties ◽  
Structure Modification ◽  
X Ray Diffraction ◽  
X Ray

Efficient Transamidation of Primary Carboxamides by in Situ Activation withN,N-Dialkylformamide Dimethyl Acetals

2006 ◽  
Vol 128 (50) ◽  
pp. 16406-16409 ◽  
Author(s):  
Thomas A. Dineen ◽  
Matthew A. Zajac ◽  
Andrew G. Myers
Keyword(s):  
In Situ Activation

In situ activation of T-lymphocytes in chronic viral and autoimmune hepatitis

1989 ◽  
Vol 9 ◽  
pp. S144
Author(s):  
H.P. Dienes ◽  
F. Autschbach ◽  
M. Wörsdörfer ◽  
S.C. Meuer ◽  
M. Manns ◽  
...  
Keyword(s):  
T Lymphocytes ◽  
Autoimmune Hepatitis ◽  
In Situ Activation

In situ activation of mouse alveolar macrophages by aerosolized liposomal IFN-gamma and muramyl tripeptide

1996 ◽  
Vol 270 (3) ◽  
pp. L429-L434 ◽  
Author(s):  
P. Goldbach ◽  
S. Dumont ◽  
R. Kessler ◽  
P. Poindron ◽  
A. Stamm
Keyword(s):  
Alveolar Macrophages ◽  
Peritoneal Macrophages ◽  
Target Cells ◽  
Tumoricidal Activity ◽  
Ifn Gamma ◽  
In Situ Activation ◽  
Organ Specific ◽  
Thawing Procedure

Interferon-gamma (IFN-gamma) was entrapped with an efficiency of 30-40% in muramyl tripeptide-containing liposomes by a freeze-thawing procedure. A microcytotoxicity assay was developed to measure the tumoricidal activity of mouse alveolar macrophages (AM) against tumoral target cells with a colorimetric viability test. Free IFN-gamma and liposomal muramyl tripeptide phosphatidylethanolamine (MTP-PE) were found to be only slightly effective to activate in vitro AM, whereas encapsulation of both INF-gamma and MTP-PE within the same liposomes produced higher activation of AM. Aerosolized IFN-gamma and liposomal immunomodulators enhanced antitumor properties of AM recovered in mice 24 h postinhalation. Whereas free IFN-gamma also induced a substantial activation of peritoneal macrophages, liposomal encapsulation significantly reduced the systemic activity of inhaled immunomodulators. This approach provides a useful model for the compartmentalized organ-specific activation of AM in mice.

A Dormant Ruthenium Catalyst Bearing a Chelating Carboxylate Ligand: In Situ Activation and Application in Metathesis Reactions

2007 ◽  
Vol 119 (38) ◽  
pp. 7344-7347 ◽  
Author(s):  
Rafał Gawin ◽  
Anna Makal ◽  
Krzysztof Woźniak ◽  
Marc Mauduit ◽  
Karol Grela
Keyword(s):  
Ruthenium Catalyst ◽  
Carboxylate Ligand ◽  
In Situ Activation ◽  
Metathesis Reactions
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