Author pages are created from data sourced from our academic publisher partnerships and public sources.
Share This Author
RNA-binding proteins: modular design for efficient function
These studies have shown how, for many RNA-binding proteins, multiple modules define the fundamental structural unit that is responsible for biological function.
Design of a Novel Globular Protein Fold with Atomic-Level Accuracy
- B. Kuhlman, G. Dantas, G. Ireton, G. Varani, B. Stoddard, D. Baker
- Medicine, PhysicsScience
- 21 November 2003
A general computational strategy that iterates between sequence design and structure prediction to design a 93-residue α/β protein called Top7 with a novel sequence and topology, found experimentally to be folded and extremely stable.
RNA recognition by a Staufen double‐stranded RNA‐binding domain
It is shown that the RNA‐binding activity of dsRBD3 is required in vivo for Staufen‐dependent localization of bicoid and oskar mRNAs.
The structure and function of small nucleolar ribonucleoproteins
- S. Reichow, T. Hamma, A. Ferré-D’Amaré, G. Varani
- Medicine, BiologyNucleic acids research
- 6 February 2007
Recent advances in the structure, assembly and function of the conserved C/D and H/ACA sno(s)RNPs are reviewed and insight is offered into the highly homologous eukaryotic snoRNPs.
Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain
- B. M. Lunde, S. Reichow, +7 authors G. Varani
- Medicine, BiologyNature Structural &Molecular Biology
- 23 July 2010
This work shows that the CIDs of two transcription termination factors, Rtt103 and Pcf11, achieve high affinity and specificity both by specifically recognizing the phosphorylated CTD and by cooperatively binding to neighboring CTD repeats.
The Cbf5–Nop10 complex is a molecular bracket that organizes box H/ACA RNPs
- T. Hamma, S. Reichow, G. Varani, A. Ferré-D’Amaré
- Biology, MedicineNature Structural &Molecular Biology
- 1 December 2005
It is found that archaeal Cbf5 can assemble with yeast Nop10 and with human telomerase RNA, consistent with the high sequence identity of the RNP components between archaea and eukarya, and the CBF5–Nop10 architecture is phylogenetically conserved.
Structure of the P1 helix from group I self-splicing introns.
The upstream cleavage site of group I self-splicing introns is identified by an absolutely conserved U.G base-pair within a double helix, explaining the great stability of RNA UUCG loops when compared with DNA loops of identical sequence, and is one of the first NMR observations of RNA 2'-OH resonances.
RNA recognition by RNP proteins during RNA processing.
Crystallographic and NMR structures of several RNP domains and a handful of structures of RNA-protein complexes have begun to reveal the molecular basis for RNP-RNA recognition.
The G x U wobble base pair. A fundamental building block of RNA structure crucial to RNA function in diverse biological systems.
The G x U wobble base pair is a fundamental unit of RNA secondary structure that is present in nearly every class of RNA from organisms of all three phylogenetic domains. It has comparable…
Solution structure of the N-terminal RNP domain of U1A protein: the role of C-terminal residues in structure stability and RNA binding.
- J. Avis, F. Allain, P. Howe, G. Varani, K. Nagai, D. Neuhaus
- Chemistry, MedicineJournal of molecular biology
- 29 March 1996
The solution structure of a fragment of the human U1A spliceosomal protein determined using multi-dimensional heteronuclear NMR is presented and the C-terminal region of the molecule is considerably more ordered in the free protein than thought previously.