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'Protein Protein Interactions' in keywords
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2001 (1)
1985 (1)
1982 (2)
1Author    JesperV. Møller, TalaatS. Mahrous, JensP. Andersen, Marc Le, MaireRequires cookie*
 Title    Functional Significance of Quaternary Organization of the Sarcoplasmic Reticulum Ca2+-ATPase  
 Abstract    There is both structural and functional evidence for protein-protein interaction between Ca2+-ATPase polypeptide chains in the sarcoplasm ic reticulum membrane. Studies on detergent solubilized ATPase indicate that the m onom eric form is capable o f performing a normal cycle o f ATP hydrolysis, but som e o f the m odulatory effects o f the substrates disappear after detergent solubilization. However, the necessity o f protein-protein interactions for the Ca2+ transport function remains unclarified. A new approach is described, em ploying A TPase reconstituted with a large excess o f phospholipid, which m ay help to resolve this question. 
  Reference    Z. Naturforsch. 37c, 517—521 (1982); received February 4 1982 
  Published    1982 
  Keywords    Sarcoplasmic Reticulum Ca2+-ATPase, Protein-Protein Interactions, Reconstitution 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0517.pdf 
 Identifier    ZNC-1982-37c-0517 
 Volume    37 
2Author    A. Ndreas Schleicher, KlausPeter HofmannRequires cookie*
 Title    Proton Uptake by Light Induced Interaction between Rhodopsin and G-Protein  
 Abstract    The light-induced proton uptake of rod outer segment disc membranes has been investigated in the absence and presence of G-protein. Proton uptake was measured as the alkalisation of the suspending medium using a pH electrode and/or the indicator dye bromocresol purple. It was found that besides the known proton uptake of photolysed rhodopsin additional uptake of one proton accompanies formation of the complex between rhodopsin and G-protein. No measurable proton uptake was found under conditions of rapid redissociation of the complex indicating an only transient protonation during its lifetime. Proton uptake was the same in washed membra­ nes recombined with G-protein and in ordinarily stacked rod outer segments. The additional proton uptake reported here is not due to enhanced metarhodopsin II. 
  Reference    Z. Naturforsch. 40c, 400—405 (1985); received January 14/February 25 1985 
  Published    1985 
  Keywords    Photoreceptor, Protein-Protein Interaction, GTP-Binding Protein, Rhodopsin 
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 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0400.pdf 
 Identifier    ZNC-1985-40c-0400 
 Volume    40 
3Author    Hans Liidi, Wilhelm HasselbachRequires cookie*
 Title    Fluorescence Studies on N-(3-Pyrene)Maleinimide-Labeled Sarcoplasmic Reticulum ATPase in Native and Solubilized Membranes  
 Abstract    Fluorescence polarization and formation of excimers were studied in N-(3-pyrene)malein-imide-labeled sarcoplasmic reticulum vesicles. 1. The polarization of pyrenemaleinimide labeled vesicles does not change with temperature and shows a pronounced decrease at labeling concentrations larger than 1 mol pyrenemaleinimide per 10 mol ATPase. 2. Solubilization of the membrane with myristoylglycerophosphocholine renders the polariza­ tion temperature dependent, but does not affect the concentration dependent depolarization observed in native vesicles. 3. The polarization of labeled vesicles is much smaller than to be expected from the tempera­ ture independent polarization indicating that the pyrenemaleinimide polarization did not monitor the rotation of the entire ATPase. Thus segmental motion occurs. 4. Pyrene excimers are observed at label concentrations larger than 1 mol label per 2.5 mol ATPase. 5. The amount of excimers was critically dependent on added detergents. From the fact that non-solubilizing amounts of myristoylglycerophosphocholine strongly reduced the amount of pyrene excimers it is concluded that in the native sarcoplasmic reticulum vesicles at least two ATPase molecules must be in close contact. 
  Reference    Z. Naturforsch. 37c, 1170 (1982); received August 16 1982 
  Published    1982 
  Keywords    Sarcoplasmic Reticulum, ATPase, Protein-Protein-Interactions, Fluorescence Polarization, Excimer Formation 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-1170.pdf 
 Identifier    ZNC-1982-37c-1170 
 Volume    37 
4Author    Jan-Wolfhard KellmannRequires cookie*
 Title    Identification of Plant Virus Movement-Host Protein Interactions  
 Abstract    A fter the discovery of 'movement proteins' as a peculiarity of plant viruses and with the help of novel methods for the detection and isolation of interacting host proteins new insights have been obtained to understand the mechanisms of virus movement in plant tissues. Rapid progress in studying the molecular mechanisms of systemic spread of plant infecting viruses revealed an interrelation between virus movement and macromolecular trafficking in plant tissues. This article summarizes current explorations on plant virus movement proteins (MPs) and introduces the state of the art in the identification and isolation of MP interacting host proteins. 
  Reference    Z. Naturforsch. 56c, 669—6 (2001); received March 1 2001 
  Published    2001 
  Keywords    Plant Viruses, Cell-to-Cell Transport, Protein-Protein Interaction 
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 TEI-XML for    default:Reihe_C/56/ZNC-2001-56c-0669.pdf 
 Identifier    ZNC-2001-56c-0669 
 Volume    56