Literature DB >> 29523707

Structure of the catalytic F1 head of the F1-Fo ATP synthase from Trypanosoma brucei.

Karen M Davies1, Werner Kühlbrandt2.   

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Year:  2018        PMID： 29523707      PMCID： PMC5879713          DOI： 10.1073/pnas.1801103115

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN： 0027-8424            Impact factor:   11.205


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  4 in total

1.  The F1-ATP synthase complex in bloodstream stage trypanosomes has an unusual and essential function.

Authors:  Achim Schnaufer; G Desmond Clark-Walker; Alodie G Steinberg; Ken Stuart
Journal:  EMBO J       Date:  2005-11-17       Impact factor: 11.598

2.  ATP synthase from Trypanosoma brucei has an elaborated canonical F1-domain and conventional catalytic sites.

Authors:  Martin G Montgomery; Ondřej Gahura; Andrew G W Leslie; Alena Zíková; John E Walker
Journal:  Proc Natl Acad Sci U S A       Date:  2018-02-12       Impact factor: 11.205

3.  In situ structure of trypanosomal ATP synthase dimer reveals a unique arrangement of catalytic subunits.

Authors:  Alexander W Mühleip; Caroline E Dewar; Achim Schnaufer; Werner Kühlbrandt; Karen M Davies
Journal:  Proc Natl Acad Sci U S A       Date:  2017-01-17       Impact factor: 11.205

4.  The F(0)F(1)-ATP synthase complex contains novel subunits and is essential for procyclic Trypanosoma brucei.

Authors:  Alena Zíková; Achim Schnaufer; Rachel A Dalley; Aswini K Panigrahi; Kenneth D Stuart
Journal:  PLoS Pathog       Date:  2009-05-15       Impact factor: 6.823
  4 in total

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