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Biology and Biochemistry

D-Index
43
Citations
8443
World Ranking
19379
National Ranking
7910

Overview

Robert S. Fuller is affiliated with the University of Michigan-Ann Arbor in the United States. Their research contributions include work in the field of obstetrics and gynecology, with recent publications focusing on public health and vaccine uptake.

Their recent work includes the paper titled "623 Dimensions of COVID-19 Vaccine Uptake in Pregnant People: A Mixed Methods Approach", published in 2024 in the American Journal of Obstetrics and Gynecology. This paper represents an analysis of vaccine acceptance patterns among pregnant populations using mixed methodologies.

Frequent co-authors who have collaborated with Robert S. Fuller include:

  • Meesha Vullikanti
  • Meghan Gerety

Publication venues for their work include:

  • American Journal of Obstetrics and Gynecology

Best Publications

  • The dnaA protein complex with the E. coli chromosomal replication origin (oriC) and other DNA sites

    Robert S. Fuller;Barbara E. Funnell;Arthur Kornberg

  • Enzymes required for yeast prohormone processing.

    Robert S. Fuller;Rachel E. Sterne;Jeremy Thorner

  • Intracellular targeting and structural conservation of a prohormone-processing endoprotease.

    Robert S. Fuller;Anthony J. Brake;Jeremy Thorner

  • Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease

    Robert S. Fuller;Anthony Brake;Jeremy Thorner

  • Enzymatic replication of the origin of the Escherichia coli chromosome.

    Robert S. Fuller;Jon M. Kaguni;Arthur Kornberg

  • Purified dnaA protein in initiation of replication at the Escherichia coli chromosomal origin of replication

    Robert S. Fuller;Arthur Kornberg

  • Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae.

    Kevin Redding;Cherie Holcomb;Robert S. Fuller

  • Localization of components involved in protein transport and processing through the yeast Golgi apparatus.

    A Franzusoff;K Redding;J Crosby;R S Fuller

  • SOI1 Encodes a Novel, Conserved Protein That Promotes TGN–Endosomal Cycling of Kex2p and Other Membrane Proteins by Modulating the Function of Two TGN Localization Signals

    Jason H. Brickner;Robert S. Fuller

  • Yeast KEX2 endopeptidase correctly cleaves a neuroendocrine prohormone in mammalian cells

    Gary Thomas;Barbara A. Thorne;Laurel Thomas;Richard G. Allen

  • Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted, soluble Kex2 protease.

    Charles Brenner;Robert S. Fuller

  • Precursor Processing by Kex2/Furin Proteases

    Nathan C. Rockwell;Damian J. Krysan;Tomoko Komiyama;Robert S. Fuller

  • Mutation of a tyrosine localization signal in the cytosolic tail of yeast Kex2 protease disrupts Golgi retention and results in default transport to the vacuole.

    C. A. Wilcox;K. Redding;R. Wright;R. S. Fuller

  • Accurate and efficient cleavage of the human insulin proreceptor by the human proprotein-processing protease furin. Characterization and kinetic parameters using the purified, secreted soluble protease expressed by a recombinant baculovirus.

    D A Bravo;J B Gleason;R I Sanchez;R A Roth

  • Posttranslational processing of the prohormone-cleaving Kex2 protease in the Saccharomyces cerevisiae secretory pathway.

    C A Wilcox;R S Fuller

  • Yapsins are a family of aspartyl proteases required for cell wall integrity in Saccharomyces cerevisiae.

    Damian J. Krysan;Elizabeth L. Ting;Claudia Abeijon;Lee Kroos

  • Quantitative characterization of furin specificity. Energetics of substrate discrimination using an internally consistent set of hexapeptidyl methylcoumarinamides.

    Damian J. Krysan;Nathan C. Rockwell;Nathan C. Rockwell;Robert S. Fuller

  • A C-terminal domain conserved in precursor processing proteases is required for intramolecular N-terminal maturation of pro-Kex2 protease.

    Pablo Gluschankof;Robert S. Fuller

  • Plasma membrane translocation of fluorescent-labeled phosphatidylethanolamine is controlled by transcription regulators, PDR1 and PDR3.

    Leslie S. Kean;Althea M. Grant;Cesar Angeletti;Yannick Mahé

  • Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease (prohormone convertase/membrane-bound protease/precursor maturation/secretory pathway/posttranslational modification)

    Robert S. Fuller;Anthony Brakes;Jeremy Thorner

Frequent Co-Authors

Arthur Kornberg
Arthur Kornberg Stanford University
Charles Brenner
Charles Brenner City Of Hope National Medical Center
Jeremy Thorner
Jeremy Thorner University of California, Berkeley
Dagmar Ringe
Dagmar Ringe Brandeis University
Robert Day
Robert Day Université de Sherbrooke
Gregory A. Petsko
Gregory A. Petsko Cornell University
Randal J. Kaufman
Randal J. Kaufman Sanford Burnham Prebys Medical Discovery Institute
Juan S. Bonifacino
Juan S. Bonifacino National Institutes of Health
Richard G. Allen
Richard G. Allen University of Idaho
William T. Dauer
William T. Dauer The University of Texas Southwestern Medical Center

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