(Q57832406)

2

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Suzette Moes

3

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Gottfried Schatz

4

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Benjamin S. Glick

https://scigraph.springernature.com/pub.10.1038/384585a0

5

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language of work or name

English

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publication date

December 1996

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published in

Nature

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volume

384

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page(s)

585-588

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issue

6609

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exact match

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cites work

Protein sorting. Pulling in the proteins

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Protein sorting in mitochondria

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The presequences of two imported mitochondrial proteins contain information for intracellular and intramitochondrial sorting

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A mitochondrial protease with two catalytic subunits of nonoverlapping specificities.

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Import of cytochrome b2 to the mitochondrial intermembrane space: the tightly folded heme-binding domain makes import dependent upon matrix ATP.

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Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism

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Successive translocation into and out of the mitochondrial matrix: targeting of proteins to the intermembrane space by a bipartite signal peptide

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[37] Reaction of protein sulfhydryl groups with Ellman's reagent.

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Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria.

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Protein import into mitochondria: the requirement for external ATP is precursor-specific whereas intramitochondrial ATP is universally needed for translocation into the matrix

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The sorting signal of cytochrome b2 promotes early divergence from the general mitochondrial import pathway and restricts the unfoldase activity of matrix Hsp70.

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Identification of a 45-kDa protein at the protein import site of the yeast mitochondrial inner membrane

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The polytopic mitochondrial inner membrane proteins MIM17 and MIM23 operate at the same preprotein import site

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The signal that sorts yeast cytochrome b2 to the mitochondrial intermembrane space contains three distinct functional regions

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A subset of non-histone nuclear proteins reversibly stabilized by the sulfhydryl cross-linking reagent tetrathionate

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High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D.

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Isolation of highly purified mitochondria from Saccharomyces cerevisiae

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A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids

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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

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New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae

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