A conserved alpha-helix at the amino terminus of prosomatostatin serves as a sorting signal for the regulated secretory pathway.
about
Conserved structural and sequence elements implicated in the processing of gene-encoded circular proteinsA prohormone convertase cleavage site within a predicted alpha-helix mediates sorting of the neuronal and endocrine polypeptide VGF into the regulated secretory pathwayCalcium-sensing receptor dimerizes in the endoplasmic reticulum: biochemical and biophysical characterization of CASR mutants retained intracellularly.Two dipolar α-helices within hormone-encoding regions of proglucagon are sorting signals to the regulated secretory pathway.Molecular and conformational basis of a specific and high-affinity interaction between AlbA and albicidin phytotoxin.An amphipathic alpha-helix in the prodomain of cocaine and amphetamine regulated transcript peptide precursor serves as its sorting signal to the regulated secretory pathway.Sorting of the neuroendocrine secretory protein Secretogranin II into the regulated secretory pathway: role of N- and C-terminal alpha-helical domains.Sending proteins to dense core secretory granules: still a lot to sort out.Role of loop structures of neuropsin in the activity of serine protease and regulated secretion.PC1/3, PC2 and PC5/6A are targeted to dense core secretory granules by a common mechanism.Dibasic cleavage site is required for sorting to the regulated secretory pathway for both pro- and neuropeptide Y.A Hydrophobic Patch in a Charged α-Helix Is Sufficient to Target Proteins to Dense Core Secretory Granules
P2860
Q28278694-1616153C-0928-4CFC-8C34-3C5E019874D0Q28573899-4D6745BF-853D-487F-ADC9-A1FD206DBFC2Q29465789-015A6E96-D44F-4122-A629-E150BE3200DBQ33652191-F98E02E7-B1C9-4E21-A436-5AF0FCA9C094Q33716416-6AF8C0D2-762A-4F6D-B526-22CD1B378C52Q34635450-480791BF-796B-4633-A303-9F2C5213EC19Q36727295-CB5CFEE1-AC83-468D-8B02-420D752D9979Q36793395-B2AC3114-A7A5-4E11-A7B0-6D116DAA997FQ38291872-B833E1A8-FEE8-4A2A-8FE6-DDD7328DB9B4Q40103701-B65AB1F0-60F8-47AE-9194-B3ABD78F73CDQ40724522-E5EB4516-40CE-4B52-BBE8-5891E9012382Q57372555-7822A428-CB05-403B-8A0D-F92E84B4C56B
P2860
A conserved alpha-helix at the amino terminus of prosomatostatin serves as a sorting signal for the regulated secretory pathway.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
A conserved alpha-helix at the ...... e regulated secretory pathway.
@en
type
label
A conserved alpha-helix at the ...... e regulated secretory pathway.
@en
prefLabel
A conserved alpha-helix at the ...... e regulated secretory pathway.
@en
P2093
P2860
P356
P1476
A conserved alpha-helix at the ...... e regulated secretory pathway.
@en
P2093
P2860
P304
26308-26316
P356
10.1074/JBC.M102514200
P407
P577
2001-04-17T00:00:00Z