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The structure of crystalline profilin–β-actin
The three-dimensional structure of bovine profilin–β-actin has been solved to 2.55 Å resolution by X-ray crystallography and appears to correspond to the solution contact in vitro. Expand
Tomato bushy stunt virus at 2.9 Å resolution
The polypeptide chain of a TBSV subunit folds into two domains, connected by a hinge, and a flexibly-linked N-terminal arm, and RNA is also not uniquely fixed to sites on the major domains. Expand
The structure of crystalline profilin-beta-actin.
The three-dimensional structure of bovine profilin-beta-actin has been solved to 2.55 A resolution by X-ray crystallography and appears to correspond to the solution contact in vitro. Expand
Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
The pattern of sequence similarity of CheY with components of other regulatory systems can be interpreted in the light of the CheY structure and supports the view that this family of proteins have a common structural motif and active site. Expand
The structure of an open state of beta-actin at 2.65 A resolution.
Applying osmotic pressure to profilin:beta-actin crystals brings about a collapse of the unit cell comparable with that seen in the open to tight-state transition, enabling an estimate of the work required to cause this transformation of beta- actin in the crystals. Expand
Crystal structure of the oligomerization domain of NSP4 from rotavirus reveals a core metal-binding site.
The crystal structure of the oligomerization domain of NSP4 which spans residues 95 to 137 is determined and this metal-binding site appears to play an important role in stabilizing the homo-tetramer, which has implications for the engagement of N SP4 as an enterotoxin. Expand
Molecular and Structural Basis for Redox Regulation of β-Actin
Abstract An essential consequence of growth factor-mediated signal transduction is the generation of intracellular H2O2. It operates as a second messenger in the control of actin microfilamentExpand
The enhancement of PCR amplification by low molecular weight amides.
This study undertook an extensive study of low molecular weight amides as a class to see how changing the substituents in the amide structure influences its effect on PCR and found several of them to be exceptionally effective and introduce them as novel PCR enhancers. Expand
The crystal structure of a major allergen from plants.
The proximity of the semi-conserved actin-binding site and the binding pocket characteristic of plant profilins suggests that epitopes encompassing both features are responsible for the cross-reactivity of antibodies between human and plantprofilins thought to be responsible for type I allergies. Expand
Crystallization and structure determination of bovine profilin at 2.0 A resolution.
The polypeptide fold of bovine profilin is generally similar to those observed by NMR forprofilin from other sources, although the N terminus of Acanthamoeba profilIn isoform I lies in a distorted helix and the C-terminal helix is less tilted with respect to the strands in the central beta-pleated sheet than is observed in bovin profil in. Expand