scholarly journals Antisense Oligonucleotides Containing an Internal, Non-Nucleotide-Based Linker Promote Site-Specific Cleavage of RNA

1996 ◽  
Vol 24 (4) ◽  
pp. 760-765 ◽  
Author(s):  
M. A. Reynolds ◽  
T. A. Beck ◽  
P. B. Say ◽  
D. A. Schwartz ◽  
B. P. Dwyer ◽  
...  
Keyword(s):  
Antisense Oligonucleotides ◽  
Site Specific

Gapmer Antisense Oligonucleotides Containing 2′,3′‐Dideoxy‐2′‐fluoro‐3′‐ C ‐hydroxymethyl‐β‐ d ‐lyxofuranosyl Nucleotides Display Site‐Specific RNase H Cleavage and Induce Gene Silencing

2020 ◽  
Vol 26 (6) ◽  
pp. 1368-1379
Author(s):  
Mathias B. Danielsen ◽  
Chenguang Lou ◽  
Jolanta Lisowiec‐Wachnicka ◽  
Anna Pasternak ◽  
Per T. Jørgensen ◽  
...  
Keyword(s):  
Gene Silencing ◽  
Antisense Oligonucleotides ◽  
Rnase H ◽  
Site Specific

Site-Specific Cleavage of RNA by a Metal-Free Artificial Nuclease Attached to Antisense Oligonucleotides

2006 ◽  
Vol 128 (24) ◽  
pp. 8063-8067 ◽  
Author(s):  
Claudio Gnaccarini ◽  
Sascha Peter ◽  
Ute Scheffer ◽  
Stefan Vonhoff ◽  
Sven Klussmann ◽  
...  
Keyword(s):  
Antisense Oligonucleotides ◽  
Site Specific ◽  
Metal Free ◽  
Artificial Nuclease

Azobenzene-modified antisense oligonucleotides for site-specific cleavage of RNA with photocontrollable property

RSC Advances ◽  
2016 ◽  
Vol 6 (96) ◽  
pp. 93398-93402 ◽  
Author(s):  
Xingyu Wang ◽  
Xingguo Liang
Keyword(s):  
Antisense Oligonucleotides ◽  
Rnase H ◽  
Rna Cleavage ◽  
Site Specific

Photoresponsive azobenzene-modified antisense oligonucleotides for site-specific RNA cleavage by RNase H.

scholarly journals Sequence-specific RNA cleavage by PNA conjugates of the metal-free artificial ribonuclease tris(2-aminobenzimidazole)

2015 ◽  
Vol 11 ◽  
pp. 493-498 ◽  
Author(s):  
Friederike Danneberg ◽  
Alice Ghidini ◽  
Plamena Dogandzhiyski ◽  
Elisabeth Kalden ◽  
Roger Strömberg ◽  
...  
Keyword(s):  
Antisense Oligonucleotides ◽  
Peptide Nucleic Acids ◽  
Substrate Recognition ◽  
Rna Degradation ◽  
Rna Cleavage ◽  
Site Specific ◽  
Substrate Specificities ◽  
Dna Conjugates ◽  
Aggregation Phenomena ◽  
Effective Site

Tris(2-aminobenzimidazole) conjugates with antisense oligonucleotides are effective site-specific RNA cleavers. Their mechanism of action is independent of metal ions. Here we investigate conjugates with peptide nucleic acids (PNA). RNA degradation occurs with similar rates and substrate specificities as in experiments with DNA conjugates we performed earlier. Although aggregation phenomena are observed in some cases, proper substrate recognition is not compromised. While our previous synthesis of 2-aminobenzimidazoles required an HgO induced cyclization step, a mercury free variant is described herein.

Large-cluster and combined fluorescent and gold immunoprobes

1996 ◽  
Vol 54 ◽  
pp. 892-893
Author(s):  
Richard D. Powell ◽  
James F. Hainfeld ◽  
Carol M. R. Halsey ◽  
David L. Spector ◽  
Shelley Kaurin ◽  
...  
Keyword(s):  
Metal Cluster ◽  
Sulfonyl Chloride ◽  
Gel Filtration ◽  
Cross Linking ◽  
Site Specific ◽  
Fab Fragments ◽  
Cluster Label ◽  
Covalently Linked ◽  
Texas Red ◽  
Fold Excess

Two new types of covalently linked, site-specific immunoprobes have been prepared using metal cluster labels, and used to stain components of cells. Combined fluorescein and 1.4 nm “Nanogold” labels were prepared by using the fluorescein-conjugated tris (aryl) phosphine ligand and the amino-substituted ligand in the synthesis of the Nanogold cluster. This cluster label was activated by reaction with a 60-fold excess of (sulfo-Succinimidyl-4-N-maleiniido-cyclohexane-l-carboxylate (sulfo-SMCC) at pH 7.5, separated from excess cross-linking reagent by gel filtration, and mixed in ten-fold excess with Goat Fab’ fragments against mouse IgG (obtained by reduction of F(ab’)2 fragments with 50 mM mercaptoethylamine hydrochloride). Labeled Fab’ fragments were isolated by gel filtration HPLC (Superose-12, Pharmacia). A combined Nanogold and Texas Red label was also prepared, using a Nanogold cluster derivatized with both and its protected analog: the cluster was reacted with an eight-fold excess of Texas Red sulfonyl chloride at pH 9.0, separated from excess Texas Red by gel filtration, then deprotected with HC1 in methanol to yield the amino-substituted label.

The challenge of detecting modifications on proteins

2020 ◽  
Vol 64 (1) ◽  
pp. 135-153 ◽  
Author(s):  
Lauren Elizabeth Smith ◽  
Adelina Rogowska-Wrzesinska
Keyword(s):  
Mass Spectrometry ◽  
Protein Function ◽  
Chemical Properties ◽  
Lysine Acetylation ◽  
Mass Determination ◽  
Post Translational Modifications ◽  
Site Specific ◽  
The Common

Abstract Post-translational modifications (PTMs) are integral to the regulation of protein function, characterising their role in this process is vital to understanding how cells work in both healthy and diseased states. Mass spectrometry (MS) facilitates the mass determination and sequencing of peptides, and thereby also the detection of site-specific PTMs. However, numerous challenges in this field continue to persist. The diverse chemical properties, low abundance, labile nature and instability of many PTMs, in combination with the more practical issues of compatibility with MS and bioinformatics challenges, contribute to the arduous nature of their analysis. In this review, we present an overview of the established MS-based approaches for analysing PTMs and the common complications associated with their investigation, including examples of specific challenges focusing on phosphorylation, lysine acetylation and redox modifications.

Sign in / Sign up

Export Citation Format

Share Document