Results 231 to 240 of about 159,783 (279)

Purification-free antifungal biocontrol platform using engineered Saccharomyces cerevisiae secreting Trichoderma atroviride chitinase. [PDF]

Bioresour Bioprocess
Song HY, Kim DH, Kim JM, Kang JY.
europepmc   +1 more source

Visualizing the translation landscape in human cells at high resolution. [PDF]

Nat Commun
Zheng W, Zhang Y, Wang J, Wang S, Chai P, Bailey EJ, Zhu C, Guo W, Devarkar SC, Wu S, Lin J, Zhang K, Liu J, Lomakin IB, Xiong Y.   +14 more
europepmc   +1 more source

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Eukaryotic elongation factor‐2 (eEF2): its regulation and peptide chain elongation

Cell Biochemistry and Function, 2011
AbstractRegulation at the level of translation in eukaryotes is feasible because of the longer lifetime of eukaryotic mRNAs in the cell. The elongation stage of mRNA translation requires a substantial amount of energy and also eukaryotic elongation factors (eEFs). The important component of eEFs, i.e.
Gautam Kaul
exaly   +3 more sources

CTP can replace GTP in reactions catalyzed by eukaryotic peptide elongation factor 1 [PDF]

FEBS Letters, 1984
In several reactions catalyzed by highly purified peptide elongation factor 1 from rabbit reticulocytes, GTP may be fully replaced by CTP but not by ATP or UTP. This holds true for the factor‐dependent binding of aminoacyl‐tRNA to ribosomes, GTPase activity, GTP‐dependent autophosphorylation of the factor protein and binding of cholesteryl 14 ...
J Hradec
exaly   +3 more sources

The S1 Factor in Peptide Chain Elongation

Nature, 1970
Aminoacyl-tRNA becomes attached to the ribosome as part of an S3 factor–GTP–aminoacyl-tRNA complex. GTP is then cleaved and an S3 factor–GDP complex is released. The S1 factor promotes the re-formation of the S3 factor–GTP–aminoacyl-tRNA complex from the S3 factor–GDP complex, aminoacyl-tRNA and GTP.
J, Waterson, G, Beaud, P, Lengyel
openaire   +2 more sources

Role of elongation factor 2 in regulating peptide-chain elongation in the heart

American Journal of Physiology-Endocrinology and Metabolism, 1994
Cardiac muscles of experimentally induced diabetic rats show a progressive decrease in the rate of protein synthesis. The decline in protein synthesis is associated with decreases in both the number and efficiency of cardiac ribosomes. In hearts from 48 h diabetic rats, the decrease in protein synthesis was accounted for solely by a 28% reduction in ...
T C, Vary, A, Nairn, C J, Lynch
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A New Concept of the Function of Elongation Factor 1 in Peptide Chain Elongation

European Journal of Biochemistry, 1976
An entirely new model for the mechanism of elongation factor 1 (EF‐1) function is presented. Experiments, in which mixtures of [3H]EF‐1, ribosomes from Krebs II ascites cells and various additional co‐factors were analyzed by chromatography on Sepharose 6B, show that EF‐1 binds to the ribosome early in the translation process and remains bound on the ...
H, Grasmuk, R D, Nolan, J, Drews
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Specificity of elongation factor EF-TU for hydrophobic peptides

Biochemical and Biophysical Research Communications, 2002
The elongation factor EF-Tu carries aminoacyl-tRNAs to the A-site of the ribosome during the elongation process of protein biosynthesis. We, and others, have recently reported that the Escherichia coli EF-Tu interacts with unfolded and denatured proteins and behaves like a chaperone in protein folding and protection against protein thermal denaturation.
Abdelharim, Malki, Teresa, Caldas, Andrea, Parmeggiani, Masamichi, Kohiyama, Gilbert, Richarme   +4 more
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A mutant of Escherichia coli blocked in peptide elongation: Altered elongation factor Ts

Journal of Molecular Biology, 1974
Abstract Among our transfer RNA-dependent growth mutants, one, HAK88, was found that carries an altered elongation factor Ts. The activity of mutant EFTs to bind GDP to EFTu, or to form the ternary complex (aminoacyl-tRNA-EFTu-GTP) is thermolabile. The effect of magnesium on the formation of EFTu-GDP from the EFTu-EFTs complex of HAK8 shows that a ...
M, Kuwano, H, Endo, T, Kamiya, K, Hori
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Peptide Elongation Factor 1 from Yeasts: Purification and Biochemical Characterization of Peptide Elongation Factors lα and 1β(α) from Saccharomyces carlsbergensis and Schizosaccharomyces pombe1

The Journal of Biochemistry, 1988
Cytoplasmic elongation factor 1 alpha (EF-1 alpha) [corrected] was purified to homogeneity in high yield from the two different yeasts Saccharomyces carlsbergensis (S. carls.) and Schizosaccharomyces pombe (S. pombe). The purification was easily achieved by CM-Sephadex column chromatography of the breakthrough fractions from DEAE-Sephadex ...
M, Miyazaki, M, Uritani, K, Fujimura, H, Yamakatsu, T, Kageyama, K, Takahashi   +5 more
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