Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20.

No abstract is available for this paper.

• Publication year

  2000

• Venue

  Cell

• Publication date

  2000-03-03

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/S0092-8674(00)80691-1PMID 10721992
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase

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  1998cited by this paper
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  1998cited by this paper
• Erratum: Functional analysis of human mitochondrial receptor Tom20 for protein import into mitochondria (Journal of Biological Chemistry (1998) 273 (26844-26851))

  1998cited by this paper
• Functional Analysis of Human Mitochondrial Receptor Tom20 for Protein Import into Mitochondria*

  1998cited by this paper
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  1998cited by this paper
• Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins

  1998cited by this paper
• Functional and structural properties of the mitochondrial outer membrane receptor Tom20.

  1998cited by this paper
• Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: evidence for the ‘acid chain’ hypothesis

  1998cited by this paper
• Characterization of the N-terminal targeting signal binding domain of the mitochondrial outer membrane receptor, Tom20.

  1998cited by this paper
• Mitochondrial preprotein translocase.

  1997cited by this paper
• Analysis of the Functional Domain of the Rat Liver Mitochondrial Import Receptor Tom20*

  1997cited by this paper
• Protein import into mitochondria.

  1997cited by this paper
• Binding of mitochondrial precursor proteins to the cytoplasmic domains of the import receptors Tom70 and Tom20 is determined by cytoplasmic chaperones

  1997cited by this paper
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  1997cited by this paper
• Just follow the acid chain

  1997cited by this paper
• Differential Recognition of Preproteins by the Purified Cytosolic Domains of the Mitochondrial Import Receptors Tom20, Tom22, and Tom70*

  1997cited by this paper
• Interactions of the Human Mitochondrial Protein Import Receptor, hTom20, with Precursor Proteins in Vitro Reveal Pleiotropic Specificities and Different Receptor Domain Requirements*

  1997cited by this paper
• Probing the environment along the protein import pathways in yeast mitochondria by site-specific photocrosslinking.

  1997cited by this paper
• MOLMOL: a program for display and analysis of macromolecular structures.

  1996cited by this paper
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  1996cited by this paper
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  1996cited by this paper
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  1995cited by this paper
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  1995cited by this paper
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  1995cited by this paper
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  1995cited by this paper
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  1995cited by this paper
• The Yeast Mitochondrial Protein Import Receptor Mas20p Binds Precursor Proteins through Electrostatic Interaction with the Positively Charged Presequence (*)

  1995cited by this paper
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  1994cited by this paper
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  1990cited by this paper
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  1990cited by this paper
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  1990cited by this paper
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  1989cited by this paper
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  1989cited by this paper
• N-terminal half of a mitochondrial presequence peptide takes a helical conformation when bound to dodecylphosphocholine micelles: a proton nuclear magnetic resonance study.

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  1988cited by this paper
• Mitochondrial presequences.

  1988cited by this paper
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  1987cited by this paper
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  1987cited by this paper
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  1986cited by this paper
• Mitochondrial targeting sequences may form amphiphilic helices.

  1986cited by this paper
• A chemically synthesized pre‐sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers.

  1986cited by this paper
• Rapid and efficient site-specific mutagenesis without phenotypic selection.

  1985cited by this paper

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