1996 - Member of the National Academy of Sciences
1993 - Fellow of the American Academy of Arts and Sciences
His scientific interests lie mostly in Biochemistry, Peptide sequence, Repressor, Biophysics and Protease. His study in Proteases, Amino acid, Endopeptidase Clp, Protein folding and Escherichia coli is carried out as part of his Biochemistry studies. His Peptide sequence research includes themes of Protein structure, Molecular biology, Binding site and Homology.
His Repressor research is multidisciplinary, incorporating perspectives in Crystallography, Operon, Stereochemistry and DNA. His work carried out in the field of Biophysics brings together such families of science as Protein degradation, Protein subunit, Mutant, Nucleotide and Unfolded protein response. Robert T. Sauer interconnects Overproduction, Periplasmic space and C-terminus in the investigation of issues within Protease.
Robert T. Sauer mainly focuses on Biochemistry, Repressor, Biophysics, Protease and Crystallography. His work in Peptide sequence, Proteases, Proteolysis, Endopeptidase Clp and Protein folding are all subfields of Biochemistry research. The concepts of his Peptide sequence study are interwoven with issues in Amino acid, Plasma protein binding, DNA-binding protein, Protein structure and Peptide.
His Repressor study combines topics from a wide range of disciplines, such as Bacteriophage, Mutant, DNA, Molecular biology and Stereochemistry. His work in Biophysics addresses subjects such as Protein degradation, which are connected to disciplines such as Unfolded protein response. While the research belongs to areas of Protease, Robert T. Sauer spends his time largely on the problem of Cell biology, intersecting his research to questions surrounding Ribosome and Signal transducing adaptor protein.
The scientist’s investigation covers issues in Biochemistry, Biophysics, Protease, Proteases and Protein degradation. His is doing research in Proteolysis, Protein subunit, Allosteric regulation, Protein folding and Plasma protein binding, both of which are found in Biochemistry. His biological study deals with issues like Protein structure, which deal with fields such as Stereochemistry.
Robert T. Sauer has researched Biophysics in several fields, including ATP hydrolysis, Crystallography, Random hexamer, Substrate and Unfolded protein response. His research in Protease intersects with topics in Translocase, Mutant and Binding site. His Proteases research integrates issues from Bacteria and Structural biology, Cell biology.
Robert T. Sauer focuses on Biochemistry, Biophysics, Proteases, Protein degradation and Protease. His study in Proteolysis, Unfolded protein response, ATP hydrolysis, Plasma protein binding and Protein folding falls under the purview of Biochemistry. The Biophysics study combines topics in areas such as Endopeptidase Clp, Escherichia coli Proteins, ATPase, Crystallography and Adenosine triphosphate.
His ATPase study deals with Protein structure intersecting with Stereochemistry. Within one scientific family, Robert T. Sauer focuses on topics pertaining to Proteasome under Protein degradation, and may sometimes address concerns connected to Function. His Protease study integrates concerns from other disciplines, such as Bacterial outer membrane and Cell biology.
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Deciphering the message in protein sequences: tolerance to amino acid substitutions
James U. Bowie;John F. Reidhaar-Olson;Wendell A. Lim;Robert T. Sauer.
Carl O. Pabo;Robert T. Sauer.
Annual Review of Biochemistry (1984)
Transcription factors: structural families and principles of DNA recognition
Carl O. Pabo;Robert T. Sauer.
Annual Review of Biochemistry (1992)
Role of a Peptide Tagging System in Degradation of Proteins Synthesized from Damaged Messenger RNA
Kenneth C. Keiler;Patrick R. H. Waller;Robert T. Sauer.
The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
Susan Gottesman;Eric Roche;YanNing Zhou;Robert T. Sauer.
Genes & Development (1998)
AAA+ proteases: ATP-fueled machines of protein destruction.
Robert T. Sauer;Tania A. Baker.
Annual Review of Biochemistry (2011)
OMP Peptide Signals Initiate the Envelope-Stress Response by Activating DegS Protease via Relief of Inhibition Mediated by Its PDZ Domain
Nathan P Walsh;Benjamin M Alba;Baundauna Bose;Carol A Gross.
Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals.
Julia M Flynn;Saskia B Neher;Yong In Kim;Robert T Sauer.
Molecular Cell (2003)
Combinatorial cassette mutagenesis as a probe of the informational content of protein sequences
John F. Reidhaar-Olson;Robert T. Sauer.
Genetic Analysis of Protein Stability and Function
Andrew A. Pakula;Robert T. Sauer.
Annual Review of Genetics (1989)
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