A novel endoplasmic reticulum export signal: proline at the +2-position from the signal peptide cleavage site.
about
The intracellular transport and secretion of calumenin-1/2 in living cells.Nesfatin-1-like peptide is a novel metabolic factor that suppresses feeding, and regulates whole-body energy homeostasis in male Wistar rats.Sar1-dependent trafficking of the human calcium receptor to the cell surface.Nucleobindin 1 is a calcium-regulated guanine nucleotide dissociation inhibitor of G{alpha}i1.Identification of novel dipeptidyl peptidase 9 substrates by two-dimensional differential in-gel electrophoresis.Enamel malformations associated with a defined dentin sialophosphoprotein mutation in two families.The evolutionary fate of alternatively spliced homologous exons after gene duplication.A DSPP mutation causing dentinogenesis imperfecta and characterization of the mutational effect.Calumenin-15 facilitates filopodia formation by promoting TGF-β superfamily cytokine GDF-15 transcription.Prediction of subcellular locations of proteins: where to proceed?Targeting endoplasmic reticulum stress in liver disease.The LPV Motif Is Essential for the Efficient Export of Secretory DMP1 From the Endoplasmic Reticulum.A model for transport of a viral membrane protein through the early secretory pathway: minimal sequence and endoplasmic reticulum lateral mobility requirements.Masking of signal sequences in CREC proteins by cDNA subcloning in epitope vectors.B-RAF and its novel negative regulator reticulocalbin 1 (RCN1) modulates cardiomyocyte hypertrophy.Surf4 (Erv29p) binds amino-terminal tripeptide motifs of soluble cargo proteins with different affinities, enabling prioritization of their exit from the endoplasmic reticulum
P2860
Q27304562-4C469870-FC5D-42FC-A336-358D0A1A4CD7Q33728555-A2C5B6BF-91C7-4FE3-9C88-83AC42349112Q33912836-4DBFC21F-3DC8-4A81-B3C3-AAF0E3391F15Q34181517-0486FEF0-F8F1-4F24-8644-5A75BABAC28AQ35691528-9DB6C901-5793-404B-A5CE-A1C3A6D33D6AQ35697998-6281D413-F56E-41C1-8524-B597F26500DDQ35826230-D595B1C8-5BE6-47DA-9B16-7E6601DABEAAQ36665293-D3DD9B27-DE4D-45A1-8E27-B6A2EBC94471Q37577453-83EA784B-B7FD-444F-9AD4-755A004756E3Q37809826-22A0E880-18D8-4CEB-93E1-40C9234E5345Q38811934-0C456AEA-A3C6-45EA-8A7B-EAB0C5D9BDDDQ38817635-B78CD823-ECFB-434B-BBD2-9A0893E7C9E9Q42242625-AD1530EE-C915-462D-A2BE-E9D2CAD5C2FCQ42699365-A5D34238-D778-44E6-824A-F92ABDE97DD6Q48752390-DEB7154A-4C81-4C6E-B01F-CC576BFF4E79Q58797063-B54E220B-74F4-4970-9429-3C1926C00342
P2860
A novel endoplasmic reticulum export signal: proline at the +2-position from the signal peptide cleavage site.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh
2009年學術文章
@zh-hant
name
A novel endoplasmic reticulum ...... signal peptide cleavage site.
@en
A novel endoplasmic reticulum ...... signal peptide cleavage site.
@nl
type
label
A novel endoplasmic reticulum ...... signal peptide cleavage site.
@en
A novel endoplasmic reticulum ...... signal peptide cleavage site.
@nl
prefLabel
A novel endoplasmic reticulum ...... signal peptide cleavage site.
@en
A novel endoplasmic reticulum ...... signal peptide cleavage site.
@nl
P2093
P2860
P356
P1476
A novel endoplasmic reticulum ...... signal peptide cleavage site.
@en
P2093
Akihiro Tomida
Sakae Saito
Satomi Tsukahara
Takashi Tsuruo
Yoshinori Tsukumo
P2860
P304
27500-27510
P356
10.1074/JBC.M109.021592
P407
P577
2009-08-05T00:00:00Z