000 01702 a2200445 4500
005 20250517133925.0
264 0 _c20180511
008 201805s 0 0 eng d
022 _a1091-6490
024 7 _a10.1073/pnas.1612386114
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aMühleip, Alexander W
245 0 0 _aIn situ structure of trypanosomal ATP synthase dimer reveals a unique arrangement of catalytic subunits.
_h[electronic resource]
260 _bProceedings of the National Academy of Sciences of the United States of America
_c01 2017
300 _a992-997 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't; Video-Audio Media
650 0 4 _aAdenosine Triphosphate
_xbiosynthesis
650 0 4 _aAmino Acid Sequence
650 0 4 _aAnimals
650 0 4 _aCatalysis
650 0 4 _aCatalytic Domain
650 0 4 _aConsensus Sequence
650 0 4 _aDimerization
650 0 4 _aEuglena gracilis
_xenzymology
650 0 4 _aMitochondria
_xenzymology
650 0 4 _aModels, Molecular
650 0 4 _aProtein Conformation
650 0 4 _aProton-Translocating ATPases
_xchemistry
650 0 4 _aProtozoan Proteins
_xchemistry
650 0 4 _aRotation
650 0 4 _aSequence Alignment
650 0 4 _aSequence Homology, Amino Acid
650 0 4 _aTrypanosoma brucei brucei
_xenzymology
700 1 _aDewar, Caroline E
700 1 _aSchnaufer, Achim
700 1 _aKühlbrandt, Werner
700 1 _aDavies, Karen M
773 0 _tProceedings of the National Academy of Sciences of the United States of America
_gvol. 114
_gno. 5
_gp. 992-997
856 4 0 _uhttps://doi.org/10.1073/pnas.1612386114
_zAvailable from publisher's website
999 _c26793025
_d26793025