(Q27618641)

2

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C Edo

3

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R J Buckanovich

4

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Y Y Yang

5

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K Musunuru

6

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R Zhong

7

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R B Darnell

8

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S K Burley

Conserved structures and diversity of functions of RNA-binding proteins

9

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publication date

15 February 1999

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published in

Structure

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volume

7

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page(s)

191-203

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issue

2

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cites work

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Nova, the paraneoplastic Ri antigen, is homologous to an RNA-binding protein and is specifically expressed in the developing motor system

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The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein

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A family of Drosophila genes encoding quaking-related maxi-KH domains.

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A novel KH-domain protein mediates cell adhesion processes in Drosophila.

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A novel ribosome-associated protein is important for efficient translation in Escherichia coli

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Cloning of a gene highly overexpressed in cancer coding for a novel KH-domain containing protein

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Vigilin, a ubiquitous protein with 14 K homology domains, is the estrogen-inducible vitellogenin mRNA 3'-untranslated region-binding protein

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MEX-3 is a KH domain protein that regulates blastomere identity in early C. elegans embryos.

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The mouse poly(C)-binding protein exists in multiple isoforms and interacts with several RNA-binding proteins

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Molecular characterization of AKAP149, a novel A kinase anchor protein with a KH domain

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Characterisation of two major cellular poly(rC)-binding human proteins, each containing three K-homologous (KH) domains

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Localized Bicaudal-C RNA encodes a protein containing a KH domain, the RNA binding motif of FMR1.

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The onconeural antigen Nova-1 is a neuron-specific RNA-binding protein, the activity of which is inhibited by paraneoplastic antibodies

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Onconeural antigens and the paraneoplastic neurologic disorders: at the intersection of cancer, immunity, and the brain

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The neuronal RNA binding protein Nova-1 recognizes specific RNA targets in vitro and in vivo

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Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome

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The solution structure of the first KH domain of FMR1, the protein responsible for the fragile X syndrome

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Probing the solution structure of the DNA-binding protein Max by a combination of proteolysis and mass spectrometry

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A point mutation in the FMR-1 gene associated with fragile X mental retardation

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Crystallizing proteins - a rational approach?

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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Purified recombinant Fmrp exhibits selective RNA binding as an intrinsic property of the fragile X mental retardation protein

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STAR, a gene family involved in signal transduction and activation of RNA.

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hnRNP proteins and the biogenesis of mRNA

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Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies.

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Evidence for a novel cytoplasmic tRNA-protein complex containing the KH-multidomain protein vigilin.

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Specific sequences in the fragile X syndrome protein FMR1 and the FXR proteins mediate their binding to 60S ribosomal subunits and the interactions among them

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FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association

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The KH domain of the branchpoint sequence binding protein determines specificity for the pre-mRNA branchpoint sequence

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Characterization and primary structure of the poly(C)-binding heterogeneous nuclear ribonucleoprotein complex K protein

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The KH domain protein encoded by quaking functions as a dimer and is essential for notochord development in Xenopus embryos

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mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3' end.

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Specificity and determinants of Sam68 RNA binding. Implications for the biological function of K homology domains

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In vitro genetic analysis of the RNA binding site of vigilin, a multi-KH-domain protein

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Mutations in gld-1, a female germ cell-specific tumor suppressor gene in Caenorhabditis elegans, affect a conserved domain also found in Src-associated protein Sam68.

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Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome

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Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin

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The three-dimensional structures of two complexes between recombinant MS2 capsids and RNA operator fragments reveal sequence-specific protein-RNA interactions

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Crystal structure of the spliceosomal U2B"-U2A' protein complex bound to a fragment of U2 small nuclear RNA

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Principles of protein-protein recognition from structure to thermodynamics

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High-accuracy molecular mass determination of proteins using matrix-assisted laser desorption mass spectrometry

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1378008

1378008

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference