Intrinsically Disordered Proteins
Mostrando 1-11 de 11 artigos, teses e dissertações.
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1. FOXP in Tetrapoda: Intrinsically Disordered Regions, Short Linear Motifs and their evolutionary significance
Abstract The FOXP subfamily is probably the most extensively characterized subfamily of the forkhead superfamily, playing important roles in development and homeostasis in vertebrates. Intrinsically disorder protein regions (IDRs) are protein segments that exhibit multiple physical interactions and play critical roles in various biological processes, includi
Genet. Mol. Biol.. Publicado em: 02/03/2017
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2. Structural analysis of human respiratory syncytial virus P protein: identification of intrinsically disordered domains
Human Respiratory Syncytial Virus P protein plus the viral RNA, N and L viral proteins, constitute the viral replication complex. In this report we describe that HRSV P protein has putative intrinsically disordered domains predicted by in silico methods. These two domains, located at the amino and caboxi terminus, were identified by mass spectrometry analysi
Brazilian Journal of Microbiology. Publicado em: 2011-03
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3. Ki-1/57 e uma proteina intrinsecamente desordenada envolvida em mecanismos de regulação genica / Ki-1/57 is an intrinsically disordered protein involved in mechanisms of gene regulation
The Ki-1/57 protein has been discovered through the cross reactivity of the monoclonal antibody Ki-1 in Hodgkin lymphoma cells. Previously, it was demonstrated that Ki-1/57 undergoes phosphorylation by PKCs and methylation by PRMT1, an arginine methyltransferase that modulates many RNA binding proteins. Here, the interaction of Ki-1/57 with RNA polyuridine a
Publicado em: 2009
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4. Expression of human respiratory syncytial virus N and P proteins: functional and immunization studies. / Expressão das proteínas N e P do vírus respiratório sincicial humano: estudos funcionais e de imunização.
The Human Respiratory Syncytial Virus is a single stranded negative RNA enveloped virus and it is considered the most important pathogen of the respiratory tract of infants and neonates. The viral N and P proteins were expressed in bacteria, purified and used for the production of polyclonal antibodies in mice. In silico studies allowed the prediction of int
Publicado em: 2009
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5. FlgM gains structure in living cells
Intrinsically disordered proteins such as FlgM play important roles in biology, but little is known about their structure in cells. We use NMR to show that FlgM gains structure inside living Escherichia coli cells and under physiologically relevant conditions in vitro, i.e., in solutions containing high concentrations (≥400 g/liter) of glucose, BSA, or ova
The National Academy of Sciences.
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6. A Self-Consistent Description of the Conformational Behavior of Chemically Denatured Proteins from NMR and Small Angle Scattering
Characterization of the conformational properties of unfolded proteins is essential for understanding the mechanisms of protein folding and misfolding. This information is also fundamental to determining the relationship between flexibility and function in the highly diverse families of intrinsically disordered proteins. Here we present a self-consistent mod
The Biophysical Society.
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7. A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides
Amyloidogenic proteins and polypeptides can be divided into two structural classes, namely those which are flexible and are intrinsically disordered in their unaggregated state and those which form a compact globular structure with a well-defined tertiary fold in their normally soluble state. This review article is focused on amyloid formation by natively di
Oxford University Press.
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8. Simulating disorder–order transitions in molecular recognition of unstructured proteins: Where folding meets binding
A microscopic study of functional disorder–order folding transitions coupled to binding is performed for the p27 protein, which derives a kinetic advantage from the intrinsically disordered unbound form on binding with the phosphorylated cyclin A-cyclin-dependent kinase 2 (Cdk2) complex. Hierarchy of structural loss during p27 coupled unfolding and unbindi
The National Academy of Sciences.
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9. α-Helical Domains Promote Translocation of Intrinsically Disordered Polypeptides into the Endoplasmic Reticulum*
Co-translational import into the endoplasmic reticulum (ER) is primarily controlled by N-terminal signal sequences that mediate targeting of the ribosome-nascent chain complex to the Sec61/translocon and initiate the translocation process. Here we show that after targeting to the translocon the secondary structure of the nascent polypeptide chain can signifi
American Society for Biochemistry and Molecular Biology.
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10. Zinc Ion-induced Domain Organization in Metallo-β-lactamases: A FLEXIBLE “ZINC ARM” FOR RAPID METAL ION TRANSFER?*
The reversible unfolding of metallo-β-lactamase from Chryseobacterium meningosepticum (BlaB) by guanidinium hydrochloride is best described by a three-state model including folded, intermediate, and unfolded states. The transformation of the folded apoenzyme into the intermediate state requires only very low denaturant concentrations, in contrast to the Zn2
American Society for Biochemistry and Molecular Biology.
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11. Structure of an Arrestin2-Clathrin Complex Reveals a Novel Clathrin Binding Domain That Modulates Receptor Trafficking*
Non-visual arrestins play a pivotal role as adaptor proteins in regulating the signaling and trafficking of multiple classes of receptors. Although arrestin interaction with clathrin, AP-2, and phosphoinositides contributes to receptor trafficking, little is known about the configuration and dynamics of these interactions. Here, we identify a novel interface
American Society for Biochemistry and Molecular Biology.