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RALPH FILLINGAME, M.D.
M.D.
Family Medicine Physician
NPI: 1760455794Individual
Specialties, Licenses & Credentials
Family Medicine PhysicianPrimary
Family Medicine
Code: 207Q00000X
MD14211(OR)
Research & Publications (20)
Aqueous accessibility to the transmembrane regions of subunit c of the Escherichia coli F1F0 ATP synthase.
PMID 19542218·J Biol Chem·2009
8-other
Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase.
PMID 18786930·J Biol Chem·2008
8-other
The cytoplasmic loops of subunit a of Escherichia coli ATP synthase may participate in the proton translocating mechanism.
PMID 18337242·J Biol Chem·2008
8-other
Subunit a facilitates aqueous access to a membrane-embedded region of subunit c in Escherichia coli F1F0 ATP synthase.
PMID 18332132·J Biol Chem·2008
8-other
Interaction of transmembrane helices in ATP synthase subunit a in solution as revealed by spin label difference NMR.
PMID 18178144·Biochim Biophys Acta·2008
8-other
Fluidity of structure and swiveling of helices in the subunit c ring of Escherichia coli ATP synthase as revealed by cysteine-cysteine cross-linking.
PMID 17893141·J Biol Chem·2007
8-other
The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c.
PMID 17766379·Protein Sci·2007
8-other
Aqueous access pathways in ATP synthase subunit a. Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5.
PMID 17234633·J Biol Chem·2007
8-other
Cross-linking between helices within subunit a of Escherichia coli ATP synthase defines the transmembrane packing of a four-helix bundle.
PMID 17035244·J Biol Chem·2006
8-other
Insights into the molecular mechanism of rotation in the Fo sector of ATP synthase.
PMID 14990464·Biophys J·2004
8-other
Backbone 1H, 15N and 13C assignments for the subunit a of the E. coli ATP synthase.
PMID 15213458·J Biomol NMR·2004
8-other
Subunit A of the E. coli ATP synthase: reconstitution and high resolution NMR with protein purified in a mixed polarity solvent.
PMID 14706821·FEBS Lett·2004
8-other
Mechanics of coupling proton movements to c-ring rotation in ATP synthase.
PMID 14630314·FEBS Lett·2003
6-review
Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane.
PMID 14595019·Proc Natl Acad Sci U S A·2003
8-other
Structural model of the transmembrane Fo rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ.
PMID 12409198·Biochim Biophys Acta·2002
4-observational
Coupling proton movements to c-ring rotation in F(1)F(o) ATP synthase: aqueous access channels and helix rotations at the a-c interface.
PMID 12206887·Biochim Biophys Acta·2002
6-review
pH dependent inactivation of solubilized F1F0 ATP synthase by dicyclohexylcarbodiimide: pK(a) of detergent unmasked aspartyl-61 in Escherichia coli subunit c.
PMID 11997138·Biochim Biophys Acta·2002
8-other
Structure of Ala24/Asp61 --> Asp24/Asn61 substituted subunit c of Escherichia coli ATP synthase: implications for the mechanism of proton transport and rotary movement in the F0 complex.
PMID 11969414·Biochemistry·2002
8-other
The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10.
PMID 11320246·Proc Natl Acad Sci U S A·2001
8-other
Data courtesy of the U.S. National Library of Medicine (NLM). Ltrl is not affiliated with or endorsed by NLM.
Contact & Hours
- Address
- 1232 UNIVERSITY OF OREGON
EUGENE, OR 97403 - Phone
- (541) 346-2770
Quick Facts
- NPI
- 1760455794
- Entity Type
- Individual
- Gender
- Male
- Medicare
- Not confirmed
- Specialties
- 1
- Locations
- 1
- Publications
- 20
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