Processing of pro-brain natriuretic peptide is suppressed by O-glycosylation in the region close to the cleavage site.
about
Natriuretic Peptides in the Regulation of Cardiovascular Physiology and Metabolic EventsFibrous dysplasia and fibroblast growth factor-23 regulationINTERACTING DISCIPLINES: Cardiac natriuretic peptides and obesity: perspectives from an endocrinologist and a cardiologistDepletion of proBNP1-108 in patients with heart failure prevents cross-reactivity with natriuretic peptidesGhrelin-like peptide with fatty acid modification and O-glycosylation in the red stingray, Dasyatis akajei.O-glycosylation modulates proprotein convertase activation of angiopoietin-like protein 3: possible role of polypeptide GalNAc-transferase-2 in regulation of concentrations of plasma lipidsSecretion of prohormone of B-type natriuretic peptide, proBNP1-108, is increased in heart failure.An antibody reactive to the Gly63-Lys68 epitope of NT-proBNP exhibits O-glycosylation-independent binding.BNP molecular forms and processing by the cardiac serine protease corin.Corin in natriuretic peptide processing and hypertensionMeasurement of nonsulfated cholecystokinins.Relationship between N-terminal pro-brain natriuretic peptide, obesity and the risk of heart failure in middle-aged German adults.Site-specific characterization of threonine, serine, and tyrosine glycosylations of amyloid precursor protein/amyloid beta-peptides in human cerebrospinal fluidGlycosylation and processing of pro-B-type natriuretic peptide in cardiomyocytes.Corin in clinical laboratory diagnosticsAberrant Glycosylation in the Left Ventricle and Plasma of Rats with Cardiac Hypertrophy and Heart Failure.Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family.Posttranslational processing of human and mouse urocortin 2: characterization and bioactivity of gene productsSecretion of glycosylated pro-B-type natriuretic peptide from normal cardiomyocytes.O-Glycosylation of a Secretory Granule Membrane Enzyme Is Essential for Its Endocytic TraffickingAnalytical Issues with Natriuretic Peptides - has this been Overly Simplified?Cardiac natriuretic peptides: from basic discovery to clinical practice.Measurement of the pro-hormone of brain type natriuretic peptide (proBNP): methodological considerations and pathophysiological relevance.MS-based approaches to unravel the molecular complexity of proprotein-derived biomarkers and support their quantification: the examples of B-type natriuretic peptide and apelin peptides.State of the art of immunoassay methods for B-type natriuretic peptides: An update.BNP in children with congenital cardiac disease: is there now sufficient evidence for its routine use?Post-translational modifications enhance NT-proBNP and BNP production in acute decompensated heart failure.Liquid chromatography-tandem mass spectrometry-based fragmentation analysis of glycopeptides.Natriuretic peptides as biomarkers of cardiac endocrine function in heart failure: new challenges and perspectives.Brain natriuretic peptide and right heart dysfunction after heart transplantation.Three molecular forms of atrial natriuretic peptides: quantitative analysis and biological characterization.A systematic study of site-specific GalNAc-type O-glycosylation modulating proprotein convertase processing.Mechanism of FGF23 processing in fibrous dysplasia.A sensor of protein O-glycosylation based on sequential processing in the Golgi apparatus.Effect of sialylated O-glycans in pro-brain natriuretic peptide stability.Will sacubitril-valsartan diminish the clinical utility of B-type natriuretic peptide testing in acute cardiac care?MiR30-GALNT1/2 Axis-Mediated Glycosylation Contributes to the Increased Secretion of Inactive Human Prohormone for Brain Natriuretic Peptide (proBNP) From Failing Hearts.Enhancement of C2C12 myoblast proliferation and differentiation by GASP-2, a myostatin inhibitorOld tool - new application: NT-proBNP in fetal medicine.Pro-B-type natriuretic peptide is cleaved intracellularly: impact of distance between O-glycosylation and cleavage sites.
P2860
Q26778333-CEA9D39A-4FEF-4DC9-86AE-2E85BBAC7467Q27010789-EA38B241-8ABE-432C-A80D-8A0BCD6A024BQ28083473-FEC868D0-5AB4-4444-AFD1-8CA26C4FCA38Q28533555-22B13BFA-6078-4E09-AB55-787BB030F468Q33517970-D94380DF-A614-46AD-BCCE-0F009A17E09DQ33691116-398515B1-7994-4BC8-A377-EFA84A7F30A9Q33994980-E92BA31A-BC57-4F91-A71F-5C9C3651330AQ34284107-75642AE6-CF99-4535-96FC-B17A096A8D21Q34369603-60D9A10B-8826-4461-885D-2D7A4FB33FA2Q34396853-215B1004-351A-428B-AE21-EBC72BB0B257Q34415302-E79D7AAD-3DFB-48FA-A5DB-059A1C85D0D6Q34571982-FEA2A0D8-EABE-429F-B90E-7619CD7F9B55Q35123119-B42D81CB-C5E4-4757-BB41-1581CF6FE2B5Q35154172-AD02CC71-9377-4C3E-A6DA-67C91D7802E3Q35634038-06977622-0501-4A10-BB15-81A5D933BBF4Q36046973-D654B131-7FD3-422A-BCA0-2F0086D2A46DQ36617733-C5EF66D4-3E18-44F7-B691-403FE15454E4Q36699526-54EE6235-DF27-4FE4-AB15-34D1E13D4CB1Q36790719-644F095E-971A-449A-8020-871049AA1EECQ36850110-FA7048F1-8DF9-43A5-A61E-D1197B1E5DA8Q37229313-7E72064E-4D2B-43FF-B241-AC35055A3CC8Q37740228-68576EE5-A6B8-432E-9F58-2522C8AC9C79Q37922195-21D77F5E-60FF-49C1-BFAA-C6F45C6A209BQ38065253-8BDD69AD-2A38-4187-894D-CD70F4BDA74DQ38303192-FB4F8427-1C54-495C-8784-F8412F5BF9D1Q38324210-2F1B18B9-1920-455B-BE77-B813DBDCE625Q38424871-DFC714C2-47A7-4706-A006-E78B09362A39Q38701314-5CFC2778-0B6A-4251-A469-60B18F5515C1Q38837698-C32574BF-C7DB-4DB6-BF14-EDFB21F65F89Q38897414-F9C78107-5189-4227-90D5-072FD8429D4EQ39102349-BAD733C1-D0CF-456A-A4C3-FFEE4EBC719DQ39244694-71A40A22-4E73-4BF3-9EA7-66C4C94B9856Q39411802-C6AC95FE-747B-4FAC-8976-D71EA91BAC24Q39540176-6149949B-B4D7-4E0A-B392-6D674713773EQ39721683-F95A495D-A71E-43D2-82FC-35B3472E9CA4Q40116429-9E33E687-BBDD-42FD-BD00-F0504543927FQ41102306-8BA45F8E-8C8A-4AAF-99E1-21453B26C81FQ41683166-15BE2776-9B2B-472C-9D0E-7B926C6E181AQ43968441-E6E6C8E6-3756-460D-9384-446FDF636BCEQ46706147-127F3D57-29F8-46A3-8E49-C25BFB7298C7
P2860
Processing of pro-brain natriuretic peptide is suppressed by O-glycosylation in the region close to the cleavage site.
description
2009 nî lūn-bûn
@nan
2009 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Processing of pro-brain natriu ...... on close to the cleavage site.
@ast
Processing of pro-brain natriu ...... on close to the cleavage site.
@en
Processing of pro-brain natriu ...... on close to the cleavage site.
@nl
type
label
Processing of pro-brain natriu ...... on close to the cleavage site.
@ast
Processing of pro-brain natriu ...... on close to the cleavage site.
@en
Processing of pro-brain natriu ...... on close to the cleavage site.
@nl
prefLabel
Processing of pro-brain natriu ...... on close to the cleavage site.
@ast
Processing of pro-brain natriu ...... on close to the cleavage site.
@en
Processing of pro-brain natriu ...... on close to the cleavage site.
@nl
P2093
P1433
P1476
Processing of pro-brain natriu ...... on close to the cleavage site.
@en
P2093
Alexander B Postnikov
Alexander G Semenov
Alexey G Katrukha
Daria V Serebryanaya
Ekaterina V Koshkina
Karina R Seferian
Marina N Bloshchitsyna
Mihail I Krasnoselsky
Natalia N Tamm
Natalia S Karpova
P304
P356
10.1373/CLINCHEM.2008.113373
P407
P577
2009-01-23T00:00:00Z