Increased Permeability of the Aquaporin SoPIP2;1 by Mercury and Mutations in Loop A

Autor: Andreas Kirscht, Sabeen Survery, Per Kjellbom, Urban Johanson

Publikováno v: Frontiers in Plant Science, Vol 7 (2016)

Aquaporins (AQPs) also referred to as Major intrinsic proteins, regulate permeability of biological membranes for water and other uncharged small polar molecules. Plants encode more AQPs than other organisms and just one of the four AQP subfamilies i

Externí odkaz: https://doaj.org/article/e430dd76a3b94e3f9a54224b8751879e

A structural preview of aquaporin 8 via homology modeling of seven vertebrate isoforms

Autor: Yonathan Sonntag, Andreas Kirscht, Urban Johanson, Per Kjellbom

Publikováno v: BMC Structural Biology, Vol 18, Iss 1, Pp 1-15 (2018)
BMC Structural Biology

Background Aquaporins (AQPs) facilitate the passage of small neutral polar molecules across membranes of the cell. In animals there are four distinct AQP subfamilies, whereof AQP8 homologues constitute one of the smallest subfamilies with just one me

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f9fb61dcb295d6389296af5fdd99b37
https://doi.org/10.1186/s12900-018-0081-8

Corrigendum: Increased Permeability of the Aquaporin SoPIP2;1 by Mercury and Mutations in Loop A

Autor: Urban Johanson, Andreas Kirscht, Per Kjellbom, Sabeen Survery

Publikováno v: Frontiers in Plant Science. 7

[This corrects the article on p. 1249 in vol. 7, PMID: 27625657.].In our Original Research article it was incorrectly stated that cadmium and mercury have a similar preference for hexagonal coordination. Although both cadmium and mercury can bind at

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce6ee0d361c13b5cc9cc38bafacf8c8b

Crystal Structure of an Ammonia-Permeable Aquaporin

Autor: Gerd Patrick Bienert, Andreas Kirscht, Poul Nissen, Bert L. de Groot, Pontus Gourdon, Urban Johanson, Shreyas S. Kaptan, François Chaumont, Per Kjellbom

Publikováno v: PLoS Biology
Kirscht, A, Kaptan, S S, Bienert, G P, Chaumont, F, Nissen, P, de Groot, B L, Kjellbom, P, Gourdon, P & Johanson, U 2016, ' Crystal Structure of an Ammonia-Permeable Aquaporin ', PLoS Biology, vol. 14, no. 3, pp. e1002411 . https://doi.org/10.1371/journal.pbio.1002411
PLoS Biology, Vol. 14, no.3, p. e1002411 (2016)
PLoS Biology, Vol 14, Iss 3, p e1002411 (2016)
PLOS Biology

Aquaporins of the TIP subfamily (Tonoplast Intrinsic Proteins) have been suggested to facilitate permeation of water and ammonia across the vacuolar membrane of plants, allowing the vacuole to efficiently sequester ammonium ions and counteract cytoso

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da4899d6a74b470146cf00ebb0222219
http://europepmc.org/articles/PMC4814140