Compact Globular Structure of Thermus thermophilus Ribosomal Protein S1 in Solution
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference19 articles.
1. Structure qnd Functions of Ribosomal Protein S1
2. Ribosomal protein S1 is required for translation of most, if not all, natural mRNAs in Escherichia coli in vivo
3. Translational initiation factors IF-1 and eIF-2α share an RNA-binding motif with prokaryotic ribosomal protein S1 and polynucleotide phosphorylase
4. The Solution Structure of the S1 RNA Binding Domain: A Member of an Ancient Nucleic Acid–Binding Fold
5. The major ribosome binding site of Escherichia coli ribosomal protein S1 is located in its N-terminal segment
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1. Comparative Analysis of Aggregation of Thermus thermophilus Ribosomal Protein bS1 and Its Stable Fragment;Biochemistry (Moscow);2020-03
2. NMR studies reveal that protein dynamics critically mediate aggregation of the well-folded and very soluble E. coli S1 ribosomal protein;2017-08-19
3. Chemosignalling, mechanotransduction and ciliary behaviour in the embryonic node: Computational evaluation of competing theories;Proceedings of the Institution of Mechanical Engineers, Part H: Journal of Engineering in Medicine;2014-04-11
4. Resonance assignment of the ribosome binding domain of E. coli ribosomal protein S1;Biomolecular NMR Assignments;2014-03-30
5. A Multi-Paradigm Modeling Framework to Simulate Dynamic Reciprocity in a Bioreactor;PLoS ONE;2013-03-29
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