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pro vyhledávání: '"Sandya Rajesh"'
Autor:
Marc Lenoir, Cansel Ustunel, Sandya Rajesh, Jaswant Kaur, Dimitri Moreau, Jean Gruenberg, Michael Overduin
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Sorting nexin 3 (SNX3) is a phosphatidylinositol 3-phosphate binding protein that localizes to early endosomes. Here the authors use NMR to resolve SNX3′s membrane interactions, revealing that membrane binding is regulated through phosphorylation o
Externí odkaz:
https://doaj.org/article/86b2c9b181b3493589dd4feb5d76f8d4
Publikováno v:
Biomolecular Nmr Assignments
Biomolecular NMR assignments
Biomolecular NMR Assignments
Biomolecular NMR assignments
Biomolecular NMR Assignments
Sorting nexin 3 (SNX3) belongs to a sub-family of sorting nexins that primarily contain a single Phox homology domain capable of binding phosphoinositides and membranes. We report the complete (1)H, (13)C and (15)N resonance assignments of the full-l
Autor:
Marc Lenoir, Sandya Rajesh, Jean Gruenberg, Dimitri Moreau, Cansel Ustunel, Jaswant Kaur, Michael Overduin
Publikováno v:
Nature Communications
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Sorting nexins anchor trafficking machines to membranes by binding phospholipids. The paradigm of the superfamily is sorting nexin 3 (SNX3), which localizes to early endosomes by recognizing phosphatidylinositol 3-phosphate (PI3P) to initiate retrome
Autor:
Gayrat Muratov, Pooja Sridhar, Sundaresan Rajesh, Elena Odintsova, Fedor Berditchevski, Sandya Rajesh, Ružica Bago, Gouri Baldwin, Michael Overduin
Publikováno v:
Journal of Biological Chemistry. 286:39606-39614
Syntenin-1 is a PDZ domain-containing adaptor that controls trafficking of transmembrane proteins including those associated with tetraspanin-enriched microdomains. We describe the interaction of syntenin-1 with ubiquitin through a novel binding site
Autor:
Derrick J. P. Squire, Denisse L. Leyton, Pooja Sridhar, Michael Overduin, Roy R. Chaudhuri, Timothy J. Knowles, Douglas F. Browning, Ashley H. Spencer, Ian R. Henderson, Sandya Rajesh, Mark Jeeves, Danielle Emery, Mark R. Viant, Ulf Sommer, Riyaz Maderbocus, Adam F. Cunningham, Eleni Manoli
Publikováno v:
EMBO reports. 12:123-128
Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential β-barrel assembly machine (Bam). Here, we report the native structure and mechanism of a core component of this complex, BamE, and show that
Autor:
Ian R. Henderson, Sandya Rajesh, Pooja Sridhar, Michael Overduin, Eleni Manoli, Timothy J. Knowles
Publikováno v:
Biomolecular NMR assignments. 4(2)
We report the (1)H, (13)C and (15)N backbone and side chain chemical shift assignments and secondary structure of the Escherichia coli protein BamE, a subunit of the BAM (Omp85) complex, the β-barrel assembly machinery present in all Gram-negative b
Publikováno v:
Biomolecular NMR assignments. 3(2)
We report the (1)H, (13)C and (15)N backbone chemical shift assignments and secondary structure of the Escherichia coli protein BamC, a 32-kDa protein subunit that forms part of the BAM (Omp85) complex, the beta-barrel assembly machinery present in a