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Featured researches published by Martha S. Briggs.


Advances in Protein Chemistry | 1986

Molecular Mechanisms of Protein Secretion: The Role of the Signal Sequence

Martha S. Briggs; Lila M. Gierasch

Publisher Summary All cells make proteins that are destined for non-cytoplasmic locations, such as the extracellular fluid, the lumina of organelles, or the cell membranes. These proteins are almost invariably synthesized in the cytoplasm. Thus, such a protein must cross or enter one or more membranes in order to reach its destination. Furthermore, this process is specific in a manner that a particular protein travels only to its proper location, and only proteins destined for a particular location are transported there. The molecular mechanism of these processes has been the subject of intense investigation in the last decade. Most knowledge concerning the secretory process has come from genetic and biochemical studies. More recently, however, biophysical techniques have been used to investigate properties of the secretory apparatus and the signal sequence. The aim of this chapter is to describe the requirement for protein secretion and also to evaluate hypotheses of the ways in which secretion occurs. Particular emphasis is given to the role of the signal sequence.


Science | 1986

Conformations of signal peptides induced by lipids suggest initial steps in protein export

Martha S. Briggs; Cornell Dg; Dluhy Ra; Lila M. Gierasch


Science | 1985

In vivo function and membrane binding properties are correlated for Escherichia coli lamB signal peptides

Martha S. Briggs; Lila M. Gierasch; Adam Zlotnick; James D. Lear; William F. DeGrado


Biochemistry | 1992

Hydrogen exchange in native and alcohol forms of ubiquitin

Yinquan Pan; Martha S. Briggs


Biochemistry | 1984

Exploring the conformational roles of signal sequences: synthesis and conformational analysis of lambda receptor protein wild-type and mutant signal peptides.

Martha S. Briggs; Lila M. Gierasch


Journal of Biological Chemistry | 1989

Functional and nonfunctional LamB signal sequences can be distinguished by their biophysical properties.

McKnight Cj; Martha S. Briggs; Lila M. Gierasch


Biochemistry | 1989

Conformations and orientations of a signal peptide interacting with phospholipid monolayers.

Cornell Dg; Dluhy Ra; Martha S. Briggs; McKnight Cj; Lila M. Gierasch


Journal of Biological Chemistry | 1987

Protein translocation into Escherichia coli membrane vesicles is inhibited by functional synthetic signal peptides.

Chen L; Phang C. Tai; Martha S. Briggs; Lila M. Gierasch


Biopolymers | 1985

Conformation–function relationships in hydrophobic peptides: Interior turns and signal sequences†

Lila M. Gierasch; A. L. Rockwell; Karyn F. Thompson; Martha S. Briggs


Protein Engineering#R##N#Applications In Science, Medicine , And Industry | 1973

11 – Physical Properties of Genetically Defined Synthetic Signal Sequences Suggest Initial Steps in Protein Export

Lila M. Gierasch; Martha S. Briggs; Donald G. Cornell

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Lila M. Gierasch

University of Massachusetts Amherst

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McKnight Cj

University of Texas Southwestern Medical Center

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Adam Zlotnick

Indiana University Bloomington

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James D. Lear

University of Pennsylvania

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Phang C. Tai

Georgia State University

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