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Larry W. Fisher - One of the best experts on this subject based on the ideXlab platform.
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Examples of starting tripeptides in soluble proteins that are predicted not to interact with Surf4/Erv29p.
2018Co-Authors: Ying Yin, Mekka R. Garcia, Alexander J. Novak, Allison M. Saunders, Raira S. Ank, Anna S. Nam, Larry W. FisherAbstract:After removal of leader sequences, amino-terminal tripeptides of TOP: vertebrate and fungal/yeast soluble ER-resident chaperone/modifying proteins and BOTTOM: vertebrate fibrillar Collagens too large to fit in standard COPII exit vesicles. Each tripeptide found in NCBI Proteins database searches (by gene name or BLASTP) is listed with vertebrate taxon notations in single letter codes at right, indicating this tripeptide was found at least one time for this taxon (e.g., M = mammal). (See S2 Table for accession number, species name, and brief representative sequence.) Color-coding based on relative contribution of each amino acid position to strength of the ER-ESCAPE motif. CALR, calreticulin; COL1A1, Collagen Type 1 alpha 1; COL2A1, Collagen Type 2 alpha 1; COL3A1, Collagen Type 3 alpha 1; COL6A1, Collagen Type 6 alpha 1; COL1A2, Collagen Type 6 alpha 2; COL6A3, Collagen Type 6 alpha 3; COL7A1, Collagen Type 7 alpha 1; COPII, coat protein complex II; ER, endoplasmic reticulum; ER-ESCAPE motif, ER-Exit by Soluble Cargo using Amino-terminal Peptide-Encoding motif; ERO1, ER oxidoreductase 1; Erv29p, ER-derived vesicles protein 29; F-GRP78, fungal glucose-regulated protein 78; GRP78, glucose-regulated protein 78; GRP94, glucose-regulated protein 94; NCBI, National Center for Biotechnology Information; PDI, protein disulfide isomerase; PDIA2, PDI family A member 2; PDIA4, PDI family A member 4; Surf4, surfeit locus protein 4; TANGO 1, transport and Golgi organization 1.
Ying Yin - One of the best experts on this subject based on the ideXlab platform.
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Examples of starting tripeptides in soluble proteins that are predicted not to interact with Surf4/Erv29p.
2018Co-Authors: Ying Yin, Mekka R. Garcia, Alexander J. Novak, Allison M. Saunders, Raira S. Ank, Anna S. Nam, Larry W. FisherAbstract:After removal of leader sequences, amino-terminal tripeptides of TOP: vertebrate and fungal/yeast soluble ER-resident chaperone/modifying proteins and BOTTOM: vertebrate fibrillar Collagens too large to fit in standard COPII exit vesicles. Each tripeptide found in NCBI Proteins database searches (by gene name or BLASTP) is listed with vertebrate taxon notations in single letter codes at right, indicating this tripeptide was found at least one time for this taxon (e.g., M = mammal). (See S2 Table for accession number, species name, and brief representative sequence.) Color-coding based on relative contribution of each amino acid position to strength of the ER-ESCAPE motif. CALR, calreticulin; COL1A1, Collagen Type 1 alpha 1; COL2A1, Collagen Type 2 alpha 1; COL3A1, Collagen Type 3 alpha 1; COL6A1, Collagen Type 6 alpha 1; COL1A2, Collagen Type 6 alpha 2; COL6A3, Collagen Type 6 alpha 3; COL7A1, Collagen Type 7 alpha 1; COPII, coat protein complex II; ER, endoplasmic reticulum; ER-ESCAPE motif, ER-Exit by Soluble Cargo using Amino-terminal Peptide-Encoding motif; ERO1, ER oxidoreductase 1; Erv29p, ER-derived vesicles protein 29; F-GRP78, fungal glucose-regulated protein 78; GRP78, glucose-regulated protein 78; GRP94, glucose-regulated protein 94; NCBI, National Center for Biotechnology Information; PDI, protein disulfide isomerase; PDIA2, PDI family A member 2; PDIA4, PDI family A member 4; Surf4, surfeit locus protein 4; TANGO 1, transport and Golgi organization 1.
Mekka R. Garcia - One of the best experts on this subject based on the ideXlab platform.
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Examples of starting tripeptides in soluble proteins that are predicted not to interact with Surf4/Erv29p.
2018Co-Authors: Ying Yin, Mekka R. Garcia, Alexander J. Novak, Allison M. Saunders, Raira S. Ank, Anna S. Nam, Larry W. FisherAbstract:After removal of leader sequences, amino-terminal tripeptides of TOP: vertebrate and fungal/yeast soluble ER-resident chaperone/modifying proteins and BOTTOM: vertebrate fibrillar Collagens too large to fit in standard COPII exit vesicles. Each tripeptide found in NCBI Proteins database searches (by gene name or BLASTP) is listed with vertebrate taxon notations in single letter codes at right, indicating this tripeptide was found at least one time for this taxon (e.g., M = mammal). (See S2 Table for accession number, species name, and brief representative sequence.) Color-coding based on relative contribution of each amino acid position to strength of the ER-ESCAPE motif. CALR, calreticulin; COL1A1, Collagen Type 1 alpha 1; COL2A1, Collagen Type 2 alpha 1; COL3A1, Collagen Type 3 alpha 1; COL6A1, Collagen Type 6 alpha 1; COL1A2, Collagen Type 6 alpha 2; COL6A3, Collagen Type 6 alpha 3; COL7A1, Collagen Type 7 alpha 1; COPII, coat protein complex II; ER, endoplasmic reticulum; ER-ESCAPE motif, ER-Exit by Soluble Cargo using Amino-terminal Peptide-Encoding motif; ERO1, ER oxidoreductase 1; Erv29p, ER-derived vesicles protein 29; F-GRP78, fungal glucose-regulated protein 78; GRP78, glucose-regulated protein 78; GRP94, glucose-regulated protein 94; NCBI, National Center for Biotechnology Information; PDI, protein disulfide isomerase; PDIA2, PDI family A member 2; PDIA4, PDI family A member 4; Surf4, surfeit locus protein 4; TANGO 1, transport and Golgi organization 1.
Alexander J. Novak - One of the best experts on this subject based on the ideXlab platform.
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Examples of starting tripeptides in soluble proteins that are predicted not to interact with Surf4/Erv29p.
2018Co-Authors: Ying Yin, Mekka R. Garcia, Alexander J. Novak, Allison M. Saunders, Raira S. Ank, Anna S. Nam, Larry W. FisherAbstract:After removal of leader sequences, amino-terminal tripeptides of TOP: vertebrate and fungal/yeast soluble ER-resident chaperone/modifying proteins and BOTTOM: vertebrate fibrillar Collagens too large to fit in standard COPII exit vesicles. Each tripeptide found in NCBI Proteins database searches (by gene name or BLASTP) is listed with vertebrate taxon notations in single letter codes at right, indicating this tripeptide was found at least one time for this taxon (e.g., M = mammal). (See S2 Table for accession number, species name, and brief representative sequence.) Color-coding based on relative contribution of each amino acid position to strength of the ER-ESCAPE motif. CALR, calreticulin; COL1A1, Collagen Type 1 alpha 1; COL2A1, Collagen Type 2 alpha 1; COL3A1, Collagen Type 3 alpha 1; COL6A1, Collagen Type 6 alpha 1; COL1A2, Collagen Type 6 alpha 2; COL6A3, Collagen Type 6 alpha 3; COL7A1, Collagen Type 7 alpha 1; COPII, coat protein complex II; ER, endoplasmic reticulum; ER-ESCAPE motif, ER-Exit by Soluble Cargo using Amino-terminal Peptide-Encoding motif; ERO1, ER oxidoreductase 1; Erv29p, ER-derived vesicles protein 29; F-GRP78, fungal glucose-regulated protein 78; GRP78, glucose-regulated protein 78; GRP94, glucose-regulated protein 94; NCBI, National Center for Biotechnology Information; PDI, protein disulfide isomerase; PDIA2, PDI family A member 2; PDIA4, PDI family A member 4; Surf4, surfeit locus protein 4; TANGO 1, transport and Golgi organization 1.
Allison M. Saunders - One of the best experts on this subject based on the ideXlab platform.
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Examples of starting tripeptides in soluble proteins that are predicted not to interact with Surf4/Erv29p.
2018Co-Authors: Ying Yin, Mekka R. Garcia, Alexander J. Novak, Allison M. Saunders, Raira S. Ank, Anna S. Nam, Larry W. FisherAbstract:After removal of leader sequences, amino-terminal tripeptides of TOP: vertebrate and fungal/yeast soluble ER-resident chaperone/modifying proteins and BOTTOM: vertebrate fibrillar Collagens too large to fit in standard COPII exit vesicles. Each tripeptide found in NCBI Proteins database searches (by gene name or BLASTP) is listed with vertebrate taxon notations in single letter codes at right, indicating this tripeptide was found at least one time for this taxon (e.g., M = mammal). (See S2 Table for accession number, species name, and brief representative sequence.) Color-coding based on relative contribution of each amino acid position to strength of the ER-ESCAPE motif. CALR, calreticulin; COL1A1, Collagen Type 1 alpha 1; COL2A1, Collagen Type 2 alpha 1; COL3A1, Collagen Type 3 alpha 1; COL6A1, Collagen Type 6 alpha 1; COL1A2, Collagen Type 6 alpha 2; COL6A3, Collagen Type 6 alpha 3; COL7A1, Collagen Type 7 alpha 1; COPII, coat protein complex II; ER, endoplasmic reticulum; ER-ESCAPE motif, ER-Exit by Soluble Cargo using Amino-terminal Peptide-Encoding motif; ERO1, ER oxidoreductase 1; Erv29p, ER-derived vesicles protein 29; F-GRP78, fungal glucose-regulated protein 78; GRP78, glucose-regulated protein 78; GRP94, glucose-regulated protein 94; NCBI, National Center for Biotechnology Information; PDI, protein disulfide isomerase; PDIA2, PDI family A member 2; PDIA4, PDI family A member 4; Surf4, surfeit locus protein 4; TANGO 1, transport and Golgi organization 1.