(Q22008506)

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P-CIP1, a novel protein that interacts with the cytosolic domain of peptidylglycine alpha-amidating monooxygenase, is associated with endosomes

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scholarly article

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P-CIP1, a novel protein that interacts with the cytosolic domain of peptidylglycine alpha-amidating monooxygenase, is associated with endosomes (English)

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Ras association domain family member 9

1 reference

GOA release 2020-03-11

endosomal transport

1 reference

GOA release 2020-03-11

author name string

L Chen

1

author given names

L

author last names

Chen

1 reference

PubMed publication ID

7 February 2023

R C Johnson

2

author given names

R C

author last names

Johnson

1 reference

PubMed publication ID

7 February 2023

S L Milgram

3

author given names

S L

author last names

Milgram

1 reference

PubMed publication ID

7 February 2023

language of work or name

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publication date

11 December 1998

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Journal of Biological Chemistry

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273

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50

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33524-32

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Novel proteins that interact with the COOH-terminal cytosolic routing determinants of an integral membrane peptide-processing enzyme

1 reference

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Proteins of synaptic vesicles involved in exocytosis and membrane recycling

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Biogenesis of constitutive secretory vesicles, secretory granules and synaptic vesicles

1 reference

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Protein targeting in the neuron

1 reference

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A molecular description of synaptic vesicle membrane trafficking

1 reference

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Peptide amidation

1 reference

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Minireview: The New Eukaryotic Precursor Processing Proteinases

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The biosynthesis of neuropeptides: peptide alpha-amidation

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Peptidylglycine alpha-amidating monooxygenase and other processing enzymes in the neurointermediate pituitary

1 reference

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Post-translational chemical modifications of proteins--III. Current developments in analytical procedures of identification and quantitation of post-translational chemically modified amino acid(s) and its derivatives

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COOH-terminal signals mediate the trafficking of a peptide processing enzyme in endocrine cells

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Identification of routing determinants in the cytosolic domain of a secretory granule-associated integral membrane protein

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The cytoplasmic domain of P-selectin contains a sorting determinant that mediates rapid degradation in lysosomes

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1 reference

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1 reference

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Expression of individual forms of peptidylglycine alpha-amidating monooxygenase in AtT-20 cells: endoproteolytic processing and routing to secretory granules

1 reference

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Differential trafficking of soluble and integral membrane secretory granule-associated proteins

1 reference

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Phosphorylation of the cytosolic domain of peptidylglycine alpha-amidating monooxygenase

1 reference

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Kalirin, a cytosolic protein with spectrin-like and GDP/GTP exchange factor-like domains that interacts with peptidylglycine alpha-amidating monooxygenase, an integral membrane peptide-processing enzyme

1 reference

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1 reference

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1 reference

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Coiled coils: new structures and new functions

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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Rab11 regulates recycling through the pericentriolar recycling endosome

1 reference

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Cytoskeletal protein ABP-280 directs the intracellular trafficking of furin and modulates proprotein processing in the endocytic pathway

1 reference

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Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes

1 reference

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Tubular early endosomal networks in AtT20 and other cells

1 reference

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Delivery of ligands from sorting endosomes to late endosomes occurs by maturation of sorting endosomes

1 reference

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Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process

1 reference

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1 reference

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1 reference

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Protein targeting via the "constitutive-like" secretory pathway in isolated pancreatic islets: passive sorting in the immature granule compartment

1 reference

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1 reference

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1 reference

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based on heuristic

inferred from DOI database lookup

Tissue specific expression of rat peptidylglycine alpha-amidating monooxygenase activity and mRNA

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.50.33524

7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

10.1074/JBC.273.50.33524

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release_sot73y7pbfgx5dci7lcc4qtc5e

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