Selection of RNA-binding peptides in vivo

Nature ◽  
1996 ◽  
Vol 380 (6570) ◽  
pp. 175-179 ◽  
Author(s):  
Kazuo Harada ◽  
Shelley S. Martin ◽  
Alan D. Frankel
Keyword(s):  
Rna Binding ◽  
Binding Peptides ◽  
Selection Of

scholarly journals In vivo selection of RNA-binding peptides from combinatorial libraries

1999 ◽  
Vol 42 (1) ◽  
pp. 213-214
Author(s):  
K. Harada ◽  
S. S. Martin ◽  
A. D. Frankel
Keyword(s):  
Rna Binding ◽  
Combinatorial Libraries ◽  
In Vivo Selection ◽  
Binding Peptides ◽  
Selection Of

Selection of RNA-Binding Peptides Using mRNA-Peptide Fusions

Methods ◽  
2001 ◽  
Vol 23 (3) ◽  
pp. 287-293 ◽  
Author(s):  
Jeffrey E. Barrick ◽  
Terry T. Takahashi ◽  
Andrey Balakin ◽  
Richard W. Roberts
Keyword(s):  
Rna Binding ◽  
Binding Peptides ◽  
Selection Of

Selection of RNA-binding peptides from combinatorial libraries

1996 ◽  
Vol 26 (3-5) ◽  
pp. 258-258
Author(s):  
Kazuo Harada ◽  
Shelley Martin ◽  
Alan D. Frankel
Keyword(s):  
Rna Binding ◽  
Combinatorial Libraries ◽  
Binding Peptides ◽  
Selection Of

scholarly journals Selection of RNA-binding peptides containing Arg-rich motif

2002 ◽  
Vol 2 (1) ◽  
pp. 281-282
Author(s):  
N. Shimada ◽  
K. Oniwa ◽  
R. Iwase ◽  
T. Yamaoka ◽  
A. Murakami
Keyword(s):  
Rna Binding ◽  
Binding Peptides ◽  
Selection Of

scholarly journals Screening in vivo for RNA-binding peptides from combinatorial libraries

2000 ◽  
Vol 44 (1) ◽  
pp. 269-270 ◽  
Author(s):  
K. Harada ◽  
S. Horiya ◽  
H. Zehavi ◽  
A. D. Frankel
Keyword(s):  
Rna Binding ◽  
Combinatorial Libraries ◽  
Binding Peptides

scholarly journals Selection of RNA-binding Peptides Containing an Arg-rich Motif

2004 ◽  
Vol 33 (3) ◽  
pp. 212-213
Author(s):  
Naohiko Shimada ◽  
Reiko Iwase ◽  
Tetsuji Yamaoka ◽  
Akira Murakami
Keyword(s):  
Rna Binding ◽  
Binding Peptides ◽  
Selection Of

Novel concatameric heparin-binding peptides reverse heparin and low-molecular-weight heparin anticoagulant activities in patient plasma in vitro and in rats in vivo

Blood ◽  
2004 ◽  
Vol 103 (4) ◽  
pp. 1356-1363 ◽  
Author(s):  
Barbara P. Schick ◽  
David Maslow ◽  
Adrianna Moshinski ◽  
James D. San Antonio
Keyword(s):  
Molecular Weight ◽  
Low Molecular Weight Heparin ◽  
Tandem Repeats ◽  
Factor Xa ◽  
Low Molecular Weight ◽  
Heparin Binding ◽  
High Affinity ◽  
Binding Peptides

Abstract Patients given unfractionated heparin (UFH) or low-molecular-weight heparin (LMWH) for prophylaxis or treatment of thrombosis sometimes suffer serious bleeding. We showed previously that peptides containing 3 or more tandem repeats of heparin-binding consensus sequences have high affinity for LMWH and neutralize LMWH (enoxaparin) in vivo in rats and in vitro in citrate. We have now modified the (ARKKAAKA)n tandem repeat peptides by cyclization or by inclusion of hydrophobic tails or cysteines to promote multimerization. These peptides exhibit high-affinity binding to LMWH (dissociation constant [Kd], ≈ 50 nM), similar potencies in neutralizing anti–Factor Xa activity of UFH and enoxaparin added to normal plasma in vitro, and efficacy equivalent to or greater than protamine. Peptide (ARKKAAKA)3VLVLVLVL was most effective in all plasmas from enoxaparin-treated patients, and was 4- to 20-fold more effective than protamine. Several other peptide structures were effective in some patients' plasmas. All high-affinity peptides reversed inhibition of thrombin-induced clot formation by UFH. These peptides (1 mg/300 g rat) neutralized 1 U/mL anti–Factor Xa activity of enoxaparin in rats within 1 to 2 minutes. Direct blood pressure and heart rate measurements showed little or no hemodynamic effect. These heparin-binding peptides, singly or in combination, are potential candidates for clinical reversal of UFH and LMWH in humans.

scholarly journals The methyltransferase SETD2 couples transcription and splicing by engaging mRNA processing factors through its SHI domain

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Saikat Bhattacharya ◽  
Michaella J. Levy ◽  
Ning Zhang ◽  
Hua Li ◽  
Laurence Florens ◽  
...  
Keyword(s):  
Rna Splicing ◽  
Rna Binding ◽  
Mrna Processing ◽  
Key Factors ◽  
Pol Ii ◽  
Mrna Transcripts ◽  
Hnrnp Protein ◽  
Processing Factors

AbstractHeterogeneous ribonucleoproteins (hnRNPs) are RNA binding molecules that are involved in key processes such as RNA splicing and transcription. One such hnRNP protein, hnRNP L, regulates alternative splicing (AS) by binding to pre-mRNA transcripts. However, it is unclear what factors contribute to hnRNP L-regulated AS events. Using proteomic approaches, we identified several key factors that co-purify with hnRNP L. We demonstrate that one such factor, the histone methyltransferase SETD2, specifically interacts with hnRNP L in vitro and in vivo. This interaction occurs through a previously uncharacterized domain in SETD2, the SETD2-hnRNP Interaction (SHI) domain, the deletion of which, leads to a reduced H3K36me3 deposition. Functionally, SETD2 regulates a subset of hnRNP L-targeted AS events. Our findings demonstrate that SETD2, by interacting with Pol II as well as hnRNP L, can mediate the crosstalk between the transcription and the splicing machinery.

Sign in / Sign up

Export Citation Format

Share Document