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Molecular basis for AU rich element recognition and

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THE J BIOLOGICAL C © 2004 by The American Society for .

Identification of TINO A NEW EVOLUTIONARILY CONSERVED BCL-2 AU-RICH ELEMENT RNA-BINDING PROTEIN* Received for publication, December 23, 2003, and in revised form, February 2, 2004 Published, JBC Papers in Press, February 9, 2004, DOI 10.1074/jbc.M314071200

Structural basis for recognition of AU-rich element ... - UC

CLICK HERE TO SEE THE SUMMARY OF CONTACTS BETWEEN HUD1,2 PROTEIN AND RNA RECOGNITION MOTIFS Reference: Wang, X and Tanaka, T. M. (2001) "Structural basis for recognition of AU-rich element RNA by he HuD protein" Nature Struc. Bio. 8, 141-145.

Malgorzata M Duszczyk - Google Scholar Citatio

This "Cited by" count includes citations to the following articles in Scholar. The ones marked * may be different from the article in the profile.

Wang, X. & Tanaka Hall, T. M. Structural basis for .

Wang, X. & Tanaka Hall, T. M. Structural basis for recognition of AU-rich element RNA by the HuD protein. Nature Struct. Biol. 8, 141-145

Multiple modes of RNA recognition by zinc finger proteins .

DNA and RNA recognition by C 2 H 2 zinc finger proteins. (a) ... hydrogen bonds with mainchain atoms are represented by green dashed lines and a transparent molecular surface is superimposed on the protein structure. ... P.E. WrightRecognition of the mRNA AU-rich element by the zinc finger domain of TIS11d. Nat Struct Mol Biol, 11 (2004), pp ...

Malgorzata M Duszczyk - Google Scholar Citatio

This "Cited by" count includes citations to the following articles in Scholar. The ones marked * may be different from the article in the profile.

Molecular basis of UG-rich RNA recognition by the human .

Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43 ... T.M. Structural basis for recognition of AU-rich element RNA by the ... S.D. et al. Molecular basis of RNA ...

Structural basis for recognition of AU-rich element RNA by .

Structural basis for recognition of AU-rich element RNA by the HuD protein. ... Molecular basis for AU-rich element recognition and dimerization by the HuR C-terminal RRM

Structural biology of poly(A) site ... - PubMed Central (PM

In the Hrp1p–Rna15p–RNA complex structure, Hrp1p interacts with the 5′ AU repeats, whereas Rna15p binds to AAUAAU at the 3′ of the RNA molecule, which illustrates the molecular basis for A-rich element recognition by Rna15p. 54 This structure also reveals a direct interaction between the RRM of Rna15p and RRM1 of Hrp1p. 54 Together with ...

RCSB PDB - 1RGO: Structural Basis for Recognition of the .

1RGO: Structural Basis for Recognition of the mRNA Class II AU-Rich Element by the Tandem Zinc Finger Domain of TIS11d. ... domain of the protein TIS11d binds to the class II AU-rich element (ARE) in the 3' untranslated region (3' UTR) of target mRNAs and promotes their deadenylation and degradation. ... Department of Molecular Biology and ...

RNA sequence- and shape-dependent recognition by proteins .

RNA sequence- and shape-dependent recognition by proteins in the ribonucleoprotein particle. scientific article. Statements. instance of ...

Scientists have provided new insights into interaction of .

A paper entitled “Molecular basis for AU-rich element recognition and dimerization by the HuR C-terminal RRM” was recently published in the journal Proceedings of the National Academy of Sciences (PNAS).

Joan Steitz, PhD > Steitz Lab | Molecular Biophysics and .

Mitton-Fry RM, DeGregorio SJ, Wang J, Steitz TA, Steitz JA. Poly(A) tail recognition by a viral RNA element through assembly of a triple helix. ... Steitz JA: Molecular basis for RNA kink-turn recognition by the h15.5K small RNP protein ... Steitz JA: The Herpesvirus saimiri small nuclear RNAs recruit AU-rich element-binding proteins but do not ...

Two ways of escaping from oxidative RNA damage: Selective .

AUF1 recognizes the AU-rich element on target RNA, and recruits the substrate to the exosome. The exosome, which contains six endoribonucleases, preforms selective degradation of target RNA. Alternatively, oxidized-RNA recognized by AUF1 might be processed through a mechanism that has not been characterized.

ZFP36L1 - Wikiped

Function. This gene is a member of the TIS11 family of early response genes.Family members are induced by various agonists such as the phorbol ester TPA and the polypeptide mitogen EGF.The gene is well conserved across species and has a promoter that contains motifs seen in other early-response genes.

Solution structure of the two RNA recognition motifs of .

Allain FH, Bouvet P, Dieckmann T, Feigon J (2000a) Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin. ... Structural basis for recognition of AU-rich element RNA by the HuD protein. Nat Struct Biol 8(2):141–145 CrossRef Google Scholar.

The transcriptional complex between the BCL2 i-motif and .

In this contribution we have identified a transcriptional factor that recognizes and binds to the BCL2 i-motif to activate transcription. The molecular basis for the recognition of the i-motif by hnRNP LL is determined, and we demonstrate that the protein unfolds the i-motif structure to form a stable single-stranded complex.

Improving the performance of the RNA AMBER force field by .

Improving the performance of the RNA AMBER force eld by tuning hydrogen bonding interactions Jiri Sponer 1 1Institute of Biophysics of the Czech Academy of Sciences, Kralovopolska 135, 612 65 Brno, Czech Republic { Czech Republic Abstract I will introduce our e orts to improve the pair-additive AMBER force eld ( ) for RNA.

Research works produced by Ryoichi Abe | Kobe University .

4 research works produced by Ryoichi Abe with 167 citations, including: Two Different RNA Binding Activities for the AU-Rich Element and the Poly(A) Sequence of the Mouse Neuronal Protein mHuC

AREsite: a database for the comprehensive investigation of .

AREsite is an online resource for the detailed investigation of AU-rich elements (ARE) in vertebrate mRNA 3′-untranslated regions (UTRs). AREs are one of the most prominent cis-acting regulatory elements found in 3′-UTRs of mRNAs.Various ARE-binding proteins that possess RNA stabilizing or destabilizing functions are recruited by sequence-specific motifs.

Table of Contents — February 19, 2019, 116 (8) | PN

Molecular basis for AU-rich element recognition and dimerization by the HuR C-terminal RRM Nina Ripin , Julien Boudet , Malgorzata M. Duszczyk , Alexandra Hinniger , Michael Faller , Miroslav Krepl , Abhilash Gadi , Robert J. Schneider , Jiří Šponer , Nicole C. Meisner-Kober , and Frédéric H.-T. Allain