हमारा समूह 1000 से अधिक वैज्ञानिक सोसायटी के सहयोग से हर साल संयुक्त राज्य अमेरिका, यूरोप और एशिया में 3000+ वैश्विक सम्मेलन श्रृंखला कार्यक्रम आयोजित करता है और 700+ ओपन एक्सेस जर्नल प्रकाशित करता है जिसमें 50000 से अधिक प्रतिष्ठित व्यक्तित्व, प्रतिष्ठित वैज्ञानिक संपादकीय बोर्ड के सदस्यों के रूप में शामिल होते हैं।
ओपन एक्सेस जर्नल्स को अधिक पाठक और उद्धरण मिल रहे हैं
700 जर्नल और 15,000,000 पाठक प्रत्येक जर्नल को 25,000+ पाठक मिल रहे हैं
Iwona K. Wower, Nusrat Jahan, Christian Zwieb and Jacek Wower
S1 is an essential protein in Escherichia coli. Although not present in all bacteria, its importance for the initiation and elongation stages of protein synthesis is well established. Beside its roles as a ribosomal protein, S1 promotes transcriptional cycling, regulates bacteriophage T4 gene expression, forms a complex with the phage. λ protein β involved in recombination, and is a subunit of the fr and Qβ RNA bacteriophage replicases. Protein S1 was also shown to bind to tmRNA, an essential component of trans-translation. Although the physiological significance of protein S1 for trans-translation has been debated for many years, recent studies clearly demonstrate that protein S1 constitutes an important, yet poorly understood component of trans-translation. We show that binding of protein S1 to the free tmRNA is a prerequisite for the association between tmRNA and stalled ribosome. S1 transits the ribosome together with the tmRNA as defective proteins are targeted for proteolysis. These findings establish protein S1 as an important target for pharmacological intervention.