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PubMed Publications| Keyword search (4,163 papers available) |  |
"Wang S" Authored Publications:
| Title | Authors | PubMed ID | |
|---|---|---|---|
| 1 | Pedestrian detection in aerial image based on convolutional neural network with attention mechanism and multi-scale prediction | Yang J; Shen J; Wang S; | 41387459 ENCS |
| 2 | Comprehensive DFT investigation of small-molecule adsorption on the paradigm M-MOF-74 family of metal-organic frameworks | Jodaeeasl N; Wang S; Hu A; Peslherbe GH; | 39829319 CERMM |
| 3 | Ammonium transporters achieve charge transfer by fragmenting their substrate | Wang S; Orabi EA; Baday S; Bernèche S; Lamoureux G; | 22631217 CERMM |
| 4 | Duplicated antagonistic EPF peptides optimize grass stomatal initiation | Jangra R; Brunetti SC; Wang X; Kaushik P; Gulick PJ; Foroud NA; Wang S; Lee JS; | 34328169 BIOLOGY |
| 5 | A polygenic score for acute vaso-occlusive pain in pediatric sickle cell disease | Rampersaud E; Kang G; Palmer LE; Rashkin SR; Wang S; Bi W; Alberts NM; Anghelescu D; Barton M; Birch K; Boulos N; Brandow AM; Brooke RJ; Chang TC; Chen W; Cheng Y; Ding J; Easton J; Hodges JR; Kanne CK; Levy S; Mulder H; Patel AP; Puri L; Rosencrance C; Rusch M; Sapkota Y; Sioson E; Sharma A; Tang X; Thrasher A; Wang W; Yao Y; Yasui Y; Yergeau D; Hankins JS; Sheehan VA; Downing JR; Estepp JH; Zhang J; DeBaun M; Wu G; Weiss MJ; | 34283174 PSYCHOLOGY |
| Title: | Ammonium transporters achieve charge transfer by fragmenting their substrate | ||||
| Authors: | Wang S, Orabi EA, Baday S, Bernèche S, Lamoureux G | ||||
| Link: | https://pubmed.ncbi.nlm.nih.gov/22631217/ | ||||
| DOI: | 10.1021/ja300129x | ||||
| Publication: | Journal of the American Chemical Society | ||||
| Keywords: | |||||
| PMID: | 22631217 | Category: | Date Added: | 2012-05-29 | |
| Dept Affiliation: |
CERMM
1 Department of Chemistry and Biochemistry and Centre for Research in Molecular Modeling (CERMM), Concordia University, 7141 Sherbrooke Street West, Montréal, Québec H4B?1R6, Canada. |
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Description: |
Proteins of the Amt/MEP family facilitate ammonium transport across the membranes of plants, fungi, and bacteria and are essential for growth in nitrogen-poor environments. Some are known to facilitate the diffusion of the neutral NH(3), while others, notably in plants, transport the positively charged NH(4)(+). On the basis of the structural data for AmtB from Escherichia coli , we illustrate the mechanism by which proteins from the Amt family can sustain electrogenic transport. Free energy calculations show that NH(4)(+) is stable in the AmtB pore, reaching a binding site from which it can spontaneously transfer a proton to a pore-lining histidine residue (His168). The substrate diffuses down the pore in the form of NH(3), while the excess proton is cotransported through a highly conserved hydrogen-bonded His168-His318 pair. This constitutes a novel permeation mechanism that confers to the histidine dyad an essential mechanistic role that was so far unknown. |
