Interacting helical faces of subunits a and c in the F(1)F(o) ATP synthase of Escherichia coli defined by disulfide cross-linking

Por Jiang, Weiping, Fillingame, Robert H.
Publicado em 1998

Chemical Reactivities of Cysteine Substitutions in Subunit a of ATP Synthase Define Residues Gating H(+) Transport from Each Side of the Membrane

Por Dong, Hui, Fillingame, Robert H.
Publicado em 2010

The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c

Por Dmitriev, Oleg Y., Fillingame, Robert H.
Publicado em 2007

Subunit a Facilitates Aqueous Access to a Membrane-embedded Region of Subunit c in Escherichia coli F(1)F(0) ATP Synthase

Por Steed, P. Ryan, Fillingame, Robert H.
Publicado em 2008

Structural Interactions between Transmembrane Helices 4 and 5 of Subunit a and the Subunit c Ring of Escherichia coli ATP Synthase

Por Moore, Kyle J., Fillingame, Robert H.
Publicado em 2008

Aqueous Accessibility to the Transmembrane Regions of Subunit c of the Escherichia coli F(1)F(0) ATP Synthase

Por Steed, P. Ryan, Fillingame, Robert H.
Publicado em 2009

Obstruction of Transmembrane Helical Movements in Subunit a Blocks Proton Pumping by F(1)F(o) ATP Synthase

Por Moore, Kyle J., Fillingame, Robert H.
Publicado em 2013

Residues in the Polar Loop of Subunit c in Escherichia coli ATP Synthase Function in Gating Proton Transport to the Cytoplasm

Por Steed, P. Ryan, Fillingame, Robert H.
Publicado em 2014

The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10

Por Jiang, Weiping, Hermolin, Joe, Fillingame, Robert H.
Publicado em 2001

Structure of the subunit c oligomer in the F(1)F(o) ATP synthase: Model derived from solution structure of the monomer and cross-linking in the native enzyme

Por Dmitriev, Oleg Y., Jones, Phil C., Fillingame, Robert H.
Publicado em 1999

Interacting cytoplasmic loops of subunits a and c of Escherichia coli F(1)F(0) ATP synthase gate H(+) transport to the cytoplasm

Por Steed, P. Ryan, Kraft, Kaitlin A., Fillingame, Robert H.
Publicado no Proc Natl Acad Sci U S A (2014)

Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane

Por Angevine, Christine M., Herold, Kelly A. G., Fillingame, Robert H.
Publicado em 2003

Insights into the Molecular Mechanism of Rotation in the F(o) Sector of ATP Synthase

Por Aksimentiev, Aleksij, Balabin, Ilya A., Fillingame, Robert H., Schulten, Klaus
Publicado em 2004

Interaction of Transmembrane Helices in ATP Synthase Subunit a in Solution as Revealed by Spin-Label Difference NMR

Por Dmitriev, Oleg Y., Freedman, Karen H., Hermolin, Joseph, Fillingame, Robert H.
Publicado em 2007

Cell-free synthesis of membrane subunits of ATP synthase in phospholipid bicelles: NMR shows subunit a fold similar to the protein in the cell membrane

Por Uhlemann, Eva-Maria E, Pierson, Hannah E, Fillingame, Robert H, Dmitriev, Oleg Y
Publicado em 2012

The Cytoplasmic Loops of Subunit a of Escherichia coli ATP Synthase May Participate in the Proton Translocating Mechanism

Por Moore, Kyle J., Angevine, Christine M., Vincent, Owen D., Schwem, Brian E., Fillingame, Robert H.
Publicado em 2008

Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linking

Por DeLeon-Rangel, Jessica, Ishmukhametov, Robert R., Jiang, Warren, Fillingame, Robert H., Vik, Steven B.
Publicado em 2013