Cold shock response in bacteria

Y Zhang, CA Gross - Annual Review of Genetics, 2021 - annualreviews.org
Bacteria often encounter temperature fluctuations in their natural habitats and must adapt to
survive. The molecular response of bacteria to sudden temperature upshift or downshift is …

RNA-binding proteins in bacteria

E Holmqvist, J Vogel - Nature Reviews Microbiology, 2018 - nature.com
RNA-binding proteins (RBPs) are central to most if not all cellular processes, dictating the
fate of virtually all RNA molecules in the cell. Starting with pioneering work on ribosomal …

CspA, the major cold-shock protein of Escherichia coli, is an RNA chaperone

W Jiang, Y Hou, M Inouye - Journal of Biological Chemistry, 1997 - ASBMB
CspA, the major cold-shock protein of Escherichia coli, is dramatically induced during the
cold-shock response. The amino acid sequence of CspA shows 43% identity to the" cold …

Polarizable force field for peptides and proteins based on the classical drude oscillator

PEM Lopes, J Huang, J Shim, Y Luo, H Li… - Journal of chemical …, 2013 - ACS Publications
Presented is a polarizable force field based on a classical Drude oscillator framework,
currently implemented in the programs CHARMM and NAMD, for modeling and molecular …

Y-box-binding protein 1 (YB-1) and its functions

IA Eliseeva, ER Kim, SG Guryanov… - Biochemistry …, 2011 - Springer
This review describes the structure and functions of Y-box binding protein 1 (YB-1) and its
homologs. Interactions of YB-1 with DNA, mRNAs, and proteins are considered. Data on the …

Microbial stress response in minimal processing

T Abee, JA Wouters - International journal of food microbiology, 1999 - Elsevier
“Bacteria have evolved adaptive networks to face the challenges of changing environments
and to survive under conditions of stress. Therefore, the efficiencies of inactivation and …

FROM FOLDING THEORIES TO FOLDING PROTEINS: A Review and Assessment of Simulation Studies of Protein Folding and Unfolding

JE Shea, CL Brooks III - Annual review of physical chemistry, 2001 - annualreviews.org
▪ Abstract Beginning with simplified lattice and continuum “minimalist” models and
progressing to detailed atomic models, simulation studies have augmented and directed …

A superfamily of proteins that contain the cold-shock domain

PL Graumann, MA Marahiel - Trends in biochemical sciences, 1998 - cell.com
Members of a family of cold-shock proteins (CSPs) are found throughout the eubacterial
domain and appear to function as RNA-chaperones. They have been implicated in various …

Folding simulations for proteins with diverse topologies are accessible in days with a physics-based force field and implicit solvent

H Nguyen, J Maier, H Huang, V Perrone… - Journal of the …, 2014 - ACS Publications
The millisecond time scale needed for molecular dynamics simulations to approach the
quantitative study of protein folding is not yet routine. One approach to extend the simulation …

[HTML][HTML] Conservation of the heterochronic regulator Lin-28, its developmental expression and microRNA complementary sites

EG Moss, L Tang - Developmental biology, 2003 - Elsevier
The heterochronic gene lin-28 is a regulator of developmental timing in the nematode
Caenorhabditis elegans. It must be expressed in the first larval stage and downregulated by …