Synapse
⌘+K
Synapse
PulseExploreClubsResearchersJournals
Instagram
HomeClubsExplore
April 1, 1988Journal of Biological ChemistryOpen Access

Directed mutations of the strongly conserved lysine 155 in the catalytic nucleotide-binding domain of beta-subunit of F1-ATPase from Escherichia coli.

View Full Paper
Ask AI
Bookmark
Share

Authors

DPDerek ParsonageWake Forest UniversityMAMarwan K. Al‐ShawiUniversity of VirginiaASA.E. SeniorAmerican University of Antigua

Discussion

Loading...

Member takes

Implication

Key Points

Key points are not available for this paper at this time.

Cite This Study

Parsonage et al. (1988) studied this question.

synapsesocial.com/papers/6a6ff759f44fa9f079dd79f4https://doi.org/10.1016/s0021-9258(18)68845-3
View Full Paper
Ask AI
Bookmark
Share

Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1The defective proton-ATPase of uncD mutants of Escherichia coli. Two mutations which affect the catalytic mechanism.1985 · 95 citations
  2. 2Structure of the nucleotide‐binding domain in the β‐subunit of Escherichia coli F1‐ATPase1986 · 108 citations
  3. 3Reaction mechanism of the membrane-bound ATPase of submitochondrial particles from beef heart.1985 · 87 citations
  4. 4Subunits of the Adenosine Triphosphatase Complex Translated In Vitro from the Escherichia coli unc Operon1980 · 118 citations
  5. 5Nuclear genes coding the yeast mitochondrial adenosine triphosphatase complex. Primary sequence analysis of ATP2 encoding the F1-ATPase beta-subunit precursor.1985 · 110 citations