Stability of Integral Membrane Proteins under High Hydrostatic Pressure: The LH2 and LH3 Antenna Pigment−Protein Complexes from Photosynthetic Bacteria

2008 ◽  
Vol 112 (26) ◽  
pp. 7948-7955 ◽  
Author(s):  
Liina Kangur ◽  
Kõu Timpmann ◽  
Arvi Freiberg
Keyword(s):  
Hydrostatic Pressure ◽  
Membrane Proteins ◽  
High Hydrostatic Pressure ◽  
Photosynthetic Bacteria ◽  
Protein Complexes ◽  
Integral Membrane Proteins ◽  
Pigment Protein Complexes ◽  
Antenna Pigment

Pigment-protein complexes of purple photosynthetic bacteria: An overview

1983 ◽  
Vol 23 (1-4) ◽  
pp. 159-169 ◽  
Author(s):  
J. Philip Thornber ◽  
Richard J. Cogdell ◽  
Beverly K. Pierson ◽  
Richard E. B. Seftor
Keyword(s):  
Photosynthetic Bacteria ◽  
Protein Complexes ◽  
Purple Photosynthetic Bacteria ◽  
Pigment Protein Complexes

scholarly journals Atypical parkinsonism–associated retromer mutant alters endosomal sorting of specific cargo proteins

2016 ◽  
Vol 214 (4) ◽  
pp. 389-399 ◽  
Author(s):  
Kirsty J. McMillan ◽  
Matthew Gallon ◽  
Adam P. Jellett ◽  
Thomas Clairfeuille ◽  
Frances C. Tilley ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Neurodegenerative Disease ◽  
Quantitative Proteomics ◽  
Protein Complexes ◽  
Integral Membrane Proteins ◽  
Atypical Parkinsonism ◽  
Endosomal Sorting ◽  
Retromer Complex ◽  
Cargo Proteins ◽  
Cargo Sorting

The retromer complex acts as a scaffold for endosomal protein complexes that sort integral membrane proteins to various cellular destinations. The retromer complex is a heterotrimer of VPS29, VPS35, and VPS26. Two of these paralogues, VPS26A and VPS26B, are expressed in humans. Retromer dysfunction is associated with neurodegenerative disease, and recently, three VPS26A mutations (p.K93E, p.M112V, and p.K297X) were discovered to be associated with atypical parkinsonism. Here, we apply quantitative proteomics to provide a detailed description of the retromer interactome. By establishing a comparative proteomic methodology, we identify how this interactome is perturbed in atypical parkinsonism-associated VPS26A mutants. In particular, we describe a selective defect in the association of VPS26A (p.K297X) with the SNX27 cargo adaptor. By showing how a retromer mutant leads to altered endosomal sorting of specific PDZ ligand–containing cargo proteins, we reveal a new mechanism for perturbed endosomal cargo sorting in atypical parkinsonism.

Spectral hole burning in pigment-protein complexes of photosynthetic bacteria

1994 ◽  
Vol 58 (1-6) ◽  
pp. 149-153 ◽  
Author(s):  
C. De Caro ◽  
R.W. Visschers ◽  
R. van Grondelle ◽  
S. Völker
Keyword(s):  
Photosynthetic Bacteria ◽  
Protein Complexes ◽  
Hole Burning ◽  
Spectral Hole Burning ◽  
Spectral Hole ◽  
Pigment Protein Complexes

Spectral hole burning study of photosynthetic antenna pigment-protein complexes

1993 ◽  
Vol 294 ◽  
pp. 131-134 ◽  
Author(s):  
M. Vácha ◽  
F. Adamec ◽  
M. Ambrož ◽  
J. Dian ◽  
J. Pšenčík ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Hole Burning ◽  
Spectral Hole Burning ◽  
Spectral Hole ◽  
Pigment Protein Complexes ◽  
Photosynthetic Antenna ◽  
Antenna Pigment
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