Results 261 to 270 of about 143,515 (300)

A Bifunctional T3SS‐Effector Simultaneously Cleaves Host MAP Kinase and Inhibits PPM1A Phosphatase

open access: yesAdvanced Science, EarlyView.
Pathogenic bacteria exploit the metalloprotease effector NleD to subvert host defenses. Structural, biochemical, and infection analyses reveal a bifunctional mechanism by which NleD binds and inhibits the host phosphatase PPM1A while preserving its proteolytic activity against MAPKs.
Yaakov Socol   +18 more
wiley   +1 more source

RNA folding in vivo

Current Opinion in Structural Biology, 2002
RNA folding in vivo is influenced by the cellular environment, the vectorial nature of transcription and translation, trans-acting factors and ion homeostasis. Specific RNA-binding proteins promote RNA folding by stabilizing the native structure or by guiding folding. In contrast, RNA chaperones, which are believed to interact nonspecifically with RNA,
Renee Schroeder, Christina Waldsich
exaly   +4 more sources

RNA FOLDING DURING TRANSCRIPTION

Annual Review of Biophysics and Biomolecular Structure, 2006
The evolution of RNA sequence needs to satisfy three requirements: folding, structure, and function. Studies on folding during transcription are related directly to folding in the cell. Understanding RNA folding during transcription requires the elucidation of structure formation and structural changes of the RNA, and the consideration of intrinsic ...
Tao Pan, Tobin R Sosnick
exaly   +3 more sources

RNA returns to the fold

Nature Chemistry, 2020
RNA has multiple roles in biology, enabled by its structural diversity. Now, artificially grafted RNA motifs have been encoded in a single RNA strand to form self-assembling nanostructures with controlled geometry and function.
Qi, Shen, Chenxiang, Lin
openaire   +2 more sources

RNA folding

Current Opinion in Structural Biology, 1995
The number of known motifs for RNA folding and RNA tertiary organization is expanding rapidly as we learn more about the diverse biological functions of RNA. Problems in protein and RNA folding have melded in recent investigations of ribonucleoprotein folding.
A M, Pyle, J B, Green
openaire   +2 more sources

Ions and RNA Folding

Annual Review of Biophysics and Biomolecular Structure, 2005
▪ Abstract  The problem of how ions influence the folding of RNA into specific tertiary structures is being addressed from both thermodynamic (by how much do different salts affect the free energy change of folding) and structural (how are ions arranged on or near an RNA and what kinds of environments do they occupy) points of view.
David E, Draper   +2 more
openaire   +2 more sources

How RNA folds

Journal of Molecular Biology, 1999
We describe the RNA folding problem and contrast it with the much more difficult protein folding problem. RNA has four similar monomer units, whereas proteins have 20 very different residues. The folding of RNA is hierarchical in that secondary structure is much more stable than tertiary folding. In RNA the two levels of folding (secondary and tertiary)
I, Tinoco, C, Bustamante
openaire   +2 more sources

RNA folding and unfolding

Current Opinion in Structural Biology, 2004
Single-molecule studies of RNA folding and unfolding are providing impressive details of the intermediates that occur and their rates of interconversion. The folding and unfolding of RNA are controlled by varying the concentration of magnesium ions and measuring fluorescence energy transfer, or by applying force to the RNA and measuring the end-to-end ...
Bibiana, Onoa, Ignacio, Tinoco
openaire   +2 more sources

A continuous analog for RNA folding

Bulletin of Mathematical Biology, 1989
A linear segment in which a number of pairs of intervals of equal length are identified as potential stems is the subject of a folding problem analogous to inference of RNA secondary structure. A quantity of free energy (or equivalently, energy per unit length) is associated with each stem, and the various types of loops are assigned energy costs as a ...
Ferretti, Vincent, Sankoff, David
openaire   +2 more sources

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