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Verrocchio, a Drosophila OB fold-containing protein, is a component of the terminin telomere-capping complex.
Results indicate that Ver is a new terminin component; it is speculated that, concomitant with telomerase loss, Drosophila evolved terminin to bind chromosome ends independently of the DNA sequence.
The implications of alternative splicing in the ENCODE protein complement
- M. Tress, P. Martelli, A. Valencia
- BiologyProceedings of the National Academy of Sciences
- 27 March 2007
It is found that alternative splicing in human genes is more frequent than has commonly been suggested, and it is demonstrated that many of the potential alternative gene products will have markedly different structure and function from their constitutively spliced counterparts.
A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin.
- D. Raimondo, G. Andreotti, A. Scaloni
- BiologyProceedings of the National Academy of Sciences…
- 3 May 2005
It is described how molecular oligomerization in aqueous solution can generate a still unknown transport form for amphipathic peptides, which is more compact and resistant to proteases than forms related to any possible monomer.
Evaluating the usefulness of protein structure models for molecular replacement
There is a correlation between the quality of models of protein structure and their suitability for molecular replacement but that the traditional method of relying on sequence identity between the model and the template used to build it is not diagnostic for the success of the procedure.
Protein function annotation by homology-based inference
Progress in the automated prediction of protein function based on protein sequence and structure is reviewed in the BioSapiens Network.
AKTIP/Ft1, a New Shelterin-Interacting Factor Required for Telomere Maintenance
It is suggested that AKTIP/Ft1 works in concert with TRF1 to facilitate telomeric DNA replication, a novel mammalian shelterin-bound factor identified on the basis of its homology with the Drosophila telomere protein Pendolino.
Toward a better understanding of the interaction between TGF-β family members and their ALK receptors
- Valentina Romano, D. Raimondo, L. Calvanese, G. D'Auria, A. Tramontano, L. Falcigno
- Biology, ChemistryJournal of Molecular Modeling
- 22 February 2012
By analyzing the surfaces of interaction in six different TGF-β/ALK complexes, this study could infer which are the structural distinctive features of the ligand-receptor binding mode and rationalize why binding of the growth factors GDF3 and Nodal to the ALK4 receptor requires the Cripto co-factor, whilst binding to theALK7 receptor does not.
Cancer-Selective Targeting of the NF-κB Survival Pathway with GADD45β/MKK7 Inhibitors
Site‐directed enzymatic PEGylation of the human granulocyte colony‐stimulating factor
A combination of computational methods allows the identification of the specific glutamines that are substrates for enzymatic PEGylation by a microbial transglutaminase, and that it is possible to rationally modify the protein and introduce PEG moieties at desired sites, thus allowing the selection of regions that are unlikely to interfere with the biological activity of a therapeutic protein.
Molecular evolution of a gene cluster of serine proteases expressed in the Anopheles gambiae female reproductive tract
The analysis of polymorphisms and divergence of these female-expressed proteases in closely related species of the A. gambiae complex revealed a high level of replacement polymorphisms consistent with relaxed evolutionary constraints of duplicated genes, allowing to rapidly fix novel replacements to perform new or more specific functions.