N-Glycosylation of Asparagine 130 in the Extracellular Domain of the Human Calcitonin Receptor Significantly Increases Peptide Hormone Affinity.

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Probing the mechanism of receptor activity-modifying protein modulation of GPCR ligand selectivity through rational design of potent adrenomedullin and calcitonin gene-related peptide antagonists.

P2860

Q49832472-FED7B632-BF03-418B-BEB8-A2AC642A86F3

P2860

N-Glycosylation of Asparagine 130 in the Extracellular Domain of the Human Calcitonin Receptor Significantly Increases Peptide Hormone Affinity.

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http://www.wikidata.org/entity/Q46350132

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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N-Glycosylation of Asparagine ...... ases Peptide Hormone Affinity.

@en

N-Glycosylation of Asparagine ...... ases Peptide Hormone Affinity.

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type

Item

label

N-Glycosylation of Asparagine ...... ases Peptide Hormone Affinity.

@en

N-Glycosylation of Asparagine ...... ases Peptide Hormone Affinity.

@nl

prefLabel

N-Glycosylation of Asparagine ...... ases Peptide Hormone Affinity.

@en

N-Glycosylation of Asparagine ...... ases Peptide Hormone Affinity.

@nl

P1476

N-Glycosylation of Asparagine ...... ases Peptide Hormone Affinity.

@en

P2093

Debbie L Hay

http://www.w3.org/2001/XMLSchema#string

Jason M Booe

http://www.w3.org/2001/XMLSchema#string

Joseph J Gingell

http://www.w3.org/2001/XMLSchema#string

Sang-Min Lee

http://www.w3.org/2001/XMLSchema#string

Virginie Sjoelund

http://www.w3.org/2001/XMLSchema#string

P2860

An amylin receptor is revealed following co-transfection of a calcitonin receptor with receptor activity modifying proteins-1 or -3

Molecular cloning and functional expression of a third isoform of the human calcitonin receptor and partial characterization of the calcitonin receptor gene

Structural basis for parathyroid hormone-related protein binding to the parathyroid hormone receptor and design of conformation-selective peptides

Crystal structure of the incretin-bound extracellular domain of a G protein-coupled receptor

Molecular recognition of parathyroid hormone by its G protein-coupled receptor

Differential structural properties of GLP-1 and exendin-4 determine their relative affinity for the GLP-1 receptor N-terminal extracellular domain.

Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product

Role of N-linked glycosylation on the function and expression of the human secretin receptor

Molecular pharmacology of the calcitonin receptor

Distinct receptor activity-modifying protein domains differentially modulate interaction with calcitonin receptors

P304

3380-3393

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scholarly article

P356

10.1021/ACS.BIOCHEM.7B00256

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P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Augen A Pioszak

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2017-06-26T00:00:00Z

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P698

28614667

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P921

glycosylation

P932

5551398

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N-Glycosylation of Asparagine 130 in the Extracellular Domain of the Human Calcitonin Receptor Significantly Increases Peptide Hormone Affinity.

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P2860

P2860

N-Glycosylation of Asparagine 130 in the Extracellular Domain of the Human Calcitonin Receptor Significantly Increases Peptide Hormone Affinity.

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type

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932