Results 271 to 280 of about 220,067 (314)
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Prediction of N-terminal protein sorting signals

Current Opinion in Structural Biology, 1997
Recently, neural networks have been applied to a widening range of problems in molecular biology. An area particularly suited to neural-network methods is the identification of protein sorting signals and the prediction of their cleavage sites, as these functional units are encoded by local, linear sequences of amino acids rather than global 3D ...
M G, Claros, S, Brunak, G, von Heijne
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Signals for Sorting of Transmembrane Proteins to Endosomes and Lysosomes

Annual Review of Biochemistry, 2003
▪ Abstract  Sorting of transmembrane proteins to endosomes and lysosomes is mediated by signals present within the cytosolic domains of the proteins. Most signals consist of short, linear sequences of amino acid residues. Some signals are referred to as tyrosine-based sorting signals and conform to the NPXY or YXXØ consensus motifs. Other signals known
Juan S, Bonifacino, Linton M, Traub
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Interaction of Tyrosine-Based Sorting Signals with Clathrin-Associated Proteins

Science, 1995
Tyrosine-based signals within the cytoplasmic domain of integral membrane proteins mediate clathrin-dependent protein sorting in the endocytic and secretory pathways. A yeast two-hybrid system was used to identify proteins that bind to tyrosine-based signals.
H, Ohno   +9 more
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Signal-mediated sorting to the regulated pathway of protein secretion

Annals of Anatomy - Anatomischer Anzeiger, 1999
The existence of specific sorting signals which direct regulated secretory proteins to secretory granules (SGs) was hypothesized two decades ago and since then has been addressed in numerous studies. The discovery that aggregation of regulated secretory proteins is involved in their sorting to SGs questioned the existence of specific sorting signals ...
H H, Gerdes, M M, Glombik
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Mitochondrial protein import in plants – Signals, Sorting, Targeting, Processing and Regulation

Plant Molecular Biology, 1998
Mitochondrial biogenesis requires a coordinated expression of both the nuclear and the organellar genomes and specific intracellular protein trafficking, processing and assembly machinery. Most mitochondrial proteins are synthesised as precursor proteins containing an N-terminal extension which functions as a targeting signal, which is proteolytically ...
E, Glaser   +3 more
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A protein complex required for signal-sequence-specific sorting and translocation

Nature, 1994
We have purified a nascent-polypeptide-associated complex (NAC) which prevents short ribosome-associated nascent polypeptides from inappropriate interactions with proteins in the cytosol. NAC binds nascent-polypeptide domains emerging from ribosomes unless a signal peptide is fully exposed. Depletion of cytosolic proteins (including NAC) from ribosomes
B, Wiedmann   +3 more
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A di‐leucine sorting signal in ZIP1 (SLC39A1) mediates endocytosis of the protein [PDF]

open access: possibleThe FEBS Journal, 2007
It has been demonstrated that the plasma membrane expression of ZIP1 is regulated by endocytic mechanisms. In the zinc‐replete condition, the level of surface expressed ZIP1 is low due to the rapid internalization of ZIP1. The present study aimed to identify a sorting signal(s) in ZIP1 that mediated endocytosis of ZIP1.
Huang, Liping, Kirschke, Catherine P
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Signal Sorting by G-Protein-Linked Receptors

1995
Publisher Summary The vast range of individual gene products encoding G-protein-linked receptors and the fact that individual neurotransmitters and hormones have, in many cases, the potential to activate multiple receptor subtypes provide the potential for exquisite control of the sensitivity of cellular response to these agents.
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Targeting signals required for protein sorting to sub-chloroplast compartments

Plant Cell Reports
Chloroplasts, distinctive subcellular organelles found exclusively in plant species, contain three membranes: the outer, inner, and thylakoid membranes. They also have three soluble compartments: the intermembrane space, stroma, and thylakoid lumen. Accordingly, delicate sorting mechanisms are required to ensure proper protein targeting to these sub ...
Ji Hyun Kang, Dong Wook Lee
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Evolution of Protein Sorting Signals

1997
Sorting signals route proteins to the correct subcellular compartment and define classes of evolutionarily conserved protein motifs. Their surprisingly low degree of sequence conservation suggests that partially functional sorting signals may arise continuously during evolution, and thus that existing proteins may be continually tested in new ...
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