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| 2. |
- Christensen, El, et al.
(författare)
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Controversies in nephrology: renal albumin handling, facts, and artifacts!
- 2007
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Ingår i: Kidney International. - : Elsevier BV. - 1523-1755 .- 0085-2538. ; 72:10, s. 1192-1194
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Forskningsöversikt (refereegranskat)abstract
- In this article, we discuss and contradict a recent publication by Russo et al., which suggests that the filtration of large amounts of albumin followed by transtubular transport of intact albumin is a physiological phenomenon.
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| 3. |
- Hebert, Hans, et al.
(författare)
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Renal, Na,K-ATPase structure from cryo-electron microscopy of two-dimensional crystals.
- 2003
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Ingår i: Annals of the New York Academy of Sciences. - 0077-8923. ; 986, s. 9-16
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Tidskriftsartikel (refereegranskat)abstract
- The molecular structure of Na,K-ATPase was determined by electron crystallography from two-dimensional crystals induced in purified membranes isolated from the outer medulla of pig kidney. The P2 type unit cell contains two protomers in the E2 conformation, each of them with a size of 65 x 75 x 150 Å3. The , ß, and subunits in the membrane crystals were demonstrated in the crystals with Western blotting and related to distinct domains in the density map. The subunit corresponds to most of the density in the transmembrane region as well as to the large hydrophilic headpiece on the cytoplasmic side of the membrane. The headpiece is divided into three separated domains. One of these gives rise to an elongated projection onto the membrane plane, while the putative nucleotide binding and phosphorylation domains form compact densities in the rest of the cytoplasmic part of the structure. Density on the extracellular face corresponds to the protein part of the ß subunit. Ten helices from the catalytic a subunit correspond to two groups of distinct densities in the transmembrane region. The structure of the lipid bilayer spanning part also suggests positions for the transmembrane helices from the ß and subunits. The overall structure of the subunit of Na,K-ATPase as determined here by cryo-electron microscopy is similar to the X-ray structure of Ca-ATPase. However, conformational changes between the E1 and E2 forms are suggested by different relative positions of cytoplasmic domains
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| 4. |
- Purhonen, P., et al.
(författare)
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Association of renal Na,K-ATPase alpha-subunit with the beta- and gamma-subunits based on cryoelectron microscopy
- 2006
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Ingår i: Journal of Membrane Biology. - : Springer Science and Business Media LLC. - 0022-2631 .- 1432-1424. ; 214:3, s. 139-146
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Tidskriftsartikel (refereegranskat)abstract
- Na,K-ATPase transports Na+ and K+ across cell membranes and consists of alpha- and beta-subunits. Na,K-ATPase also associates with small FXYD proteins that regulate the activity of the pump. We have used cryoelectron microscopy of two-dimensional crystals including data to 8 A resolution to determine the three-dimensional (3-D) structure of renal Na,K-ATPase containing FXYD2, the gamma-subunit. A homology model for the a- subunit was calculated from a Ca2+-ATPase structure and used to locate the additional beta- and gamma-subunits present in the 3-D map of Na,K-ATPase. Based on the 3-D map, the beta- subunit is located close to transmembrane helices M8 and M10 and the gamma-subunit is adjacent to helices M2 and M9 of the alpha-subunit.
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