Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Priyadarsini, Kadirvel"'
Autor:
Ahalyaa Subramanian, Priyadarsini Kadirvel, Niranjana Sridharan, Sharmila Anishetty, Sreelakshmi Subramanian, Senthamizhan Vimaladhasan
Publikováno v:
Journal of Biomolecular Structure and Dynamics. :1-12
Iron-sulfur (Fe-S) clusters are one of the earliest known metal complexes in biological molecules. Suf system is one of the Fe-S biogenesis pathways. SufA belongs to the Suf pathway. It is an A-type carrier protein that transfers Fe-S clusters from t
Publikováno v:
Carbohydrate Research. 480:42-53
Sulfolobus solfataricus β-glycosidase (SS-βGly) belongs to Glycosyl Hydrolase family1 (GH1) with broad substrate specificity. SS-βGly catalyzes both hydrolysis and transglycosylation reactions. SS-βGly is commonly used to synthesize variety of ga
Autor:
Priyadarsini, Kadirvel, Ahalyaa, Subramanian, Niranjana, Sridharan, Sreelakshmi, Subramanian, Senthamizhan, Vimaladhasan, Sharmila, Anishetty
Publikováno v:
Journal of biomolecular structuredynamics. 39(9)
Iron-sulfur (Fe-S) clusters are one of the earliest known metal complexes in biological molecules. Suf system is one of the Fe-S biogenesis pathways. SufA belongs to the Suf pathway. It is an A-type carrier protein that transfers Fe-S clusters from t
Autor:
Priyadarsini Kadirvel, Ahalyaa Subramanian, Niranjana Sridharan, Sreelakshmi Subramanian, Senthamizhan Vimaladhasan, Anishetty, Sharmila
Iron-sulfur (Fe-S) clusters are one of the earliest known metal complexes in biological molecules. Suf system is one of the Fe-S biogenesis pathways. SufA belongs to the Suf pathway. It is an A-type carrier protein that transfers Fe-S clusters from t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::522a9eccbeb4b1373f062d7cc2e2638e
Publikováno v:
Journal of cellular biochemistry. 119(4)
Profilin is one of the actin-binding proteins that regulate dynamics of actin polymerization. It plays a key role in cell motility and invasion. It also interacts with several other proteins notably through its poly-L-proline (PLP) binding site. Prof