Mühleip, Alexander W <br/><br/>
In situ structure of trypanosomal ATP synthase dimer reveals a unique arrangement of catalytic subunits.  [electronic resource] 

 -  Proceedings of the National Academy of Sciences of the United States of America  01 2017 
 - 992-997 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Video-Audio Media 
<br/><br/><label>ISSN: </label>1091-6490 
<br/><br/><label>Standard No.: </label>10.1073/pnas.1612386114  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Adenosine Triphosphate--biosynthesis<br/>Amino Acid Sequence<br/>Animals<br/>Catalysis<br/>Catalytic Domain<br/>Consensus Sequence<br/>Dimerization<br/>Euglena gracilis--enzymology<br/>Mitochondria--enzymology<br/>Models, Molecular<br/>Protein Conformation<br/>Proton-Translocating ATPases--chemistry<br/>Protozoan Proteins--chemistry<br/>Rotation<br/>Sequence Alignment<br/>Sequence Homology, Amino Acid<br/>Trypanosoma brucei brucei--enzymology