Ras Mulinta
University of Alberta
4 Papers
64 Citations
Ras Mulinta is an academic researcher from University of Alberta. The author has contributed to research in topics: Concentrative nucleoside transporter & Cotransporter. The author has an hindex of 4, co-authored 4 publications.
Chat about Author
Papers
Conserved glutamate residues are critically involved in Na+/nucleoside cotransport by human concentrative nucleoside transporter 1 (hCNT1).
Sylvia Y.M. Yao,Amy M. L. Ng,Melissa D. Slugoski,Kyla M. Smith,Ras Mulinta,Edward Karpinski,Carol E. Cass,Carol E. Cass,Stephen A. Baldwin,James D. Young +9 more
TL;DR: Findings demonstrate roles for Glu-308,Glu-322, and GLU-498 in Na+/nucleoside cotransport and suggest locations within a common cation/n nucleoside translocation pore.
19
A conformationally mobile cysteine residue (Cys-561) modulates Na+ and H+ activation of human CNT3.
Melissa D. Slugoski,Kyla M. Smith,Ras Mulinta,Amy M. L. Ng,Sylvia Y.M. Yao,Ellen Morrison,Queenie O.T. Lee,Jing Zhang,Jing Zhang,Edward Karpinski,Carol E. Cass,Carol E. Cass,Stephen A. Baldwin,James D. Young +13 more
TL;DR: The present investigation validates hCNT3C- as a template for substituted cysteine accessibility method studies of CNTs and reveals a pivotal functional role for Cys-561 in Na+- as well as H+-coupled modes of hC NT3 nucleoside transport.
18
Substituted cysteine accessibility method (SCAM) analysis of the transport domain of human concentrative nucleoside transporter 3 (hCNT3) and other family members reveals features of structural and functional importance
TL;DR: Results validate the newly developed structural homology model of CNT membrane architecture for human CNTs, revealed extended conformationally mobile regions within transport-domain TMs, identified pore-lining residues of functional importance, and provided evidence of an emerging novel elevator-type mechanism of transporter function.
15
Substituted cysteine accessibility method analysis of human concentrative nucleoside transporter hCNT3 reveals a novel discontinuous region of functional importance within the CNT family motif (G/A)XKX3NEFVA(Y/M/F).
Melissa D. Slugoski,Amy M. L. Ng,Sylvia Y.M. Yao,Colin C. Lin,Ras Mulinta,Carol E. Cass,Carol E. Cass,Stephen A. Baldwin,James D. Young +8 more
TL;DR: A novel membrane-associated topology for a region of the protein (TM 11A) that includes the highly conserved CNT family motif (G/A)XKX3NEFVA(Y/M/F) is suggested to suggest a new revised 15-TM CNT membrane architecture.
13