Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: identity with Rinderknecht's enzyme Y - Wikidata - wikimedia - TriplyDB

Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: identity with Rinderknecht's enzyme Y

Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: identity with Rinderknecht's enzyme Y

http://www.wikidata.org/entity/Q24675338

about

Uncertainties in the classification of human cationic trypsinogen (PRSS1) variants as hereditary pancreatitis-associated mutations Chymotrypsin C (CTRC) variants that diminish activity or secretion are associated with chronic pancreatitis Hereditary pancreatitis caused by mutation-induced misfolding of human cationic trypsinogen: a novel disease mechanism Caldecrin: A pancreas-derived hypocalcemic factor, regulates osteoclast formation and function Framework for interpretation of trypsin-antitrypsin imbalance and genetic heterogeneity in pancreatitis Genetics of pancreatitis Pancreatic cancer risk in hereditary pancreatitis Long-range Electrostatic Complementarity Governs Substrate Recognition by Human Chymotrypsin C, a Key Regulator of Digestive Enzyme Activation Chymotrypsin C mutations in chronic pancreatitis.A conservative assessment of the major genetic causes of idiopathic chronic pancreatitis: data from a comprehensive analysis of PRSS1, SPINK1, CTRC and CFTR genes in 253 young French patients Pancreatitis-associated chymotrypsinogen C (CTRC) mutant elicits endoplasmic reticulum stress in pancreatic acinar cells Genetic Risk in Chronic Pancreatitis: The Trypsin-Dependent Pathway.High affinity small protein inhibitors of human chymotrypsin C (CTRC) selected by phage display reveal unusual preference for P4' acidic residues.Chymotrypsin C is a co-activator of human pancreatic procarboxypeptidases A1 and A2.Genetics of acute and chronic pancreatitis: An update.Genetic and phenotypic heterogeneity in tropical calcific pancreatitis Gene conversion between cationic trypsinogen (PRSS1) and the pseudogene trypsinogen 6 (PRSS3P2) in patients with chronic pancreatitis.Chymotrypsin C (caldecrin) is associated with enamel development The Common Chymotrypsinogen C (CTRC) Variant G60G (C.180T) Increases Risk of Chronic Pancreatitis But Not Recurrent Acute Pancreatitis in a North American Population.Mesotrypsin Signature Mutation in a Chymotrypsin C (CTRC) Variant Associated with Chronic Pancreatitis.Increased activation of hereditary pancreatitis-associated human cationic trypsinogen mutants in presence of chymotrypsin C Glycomic and proteomic profiling of pancreatic cyst fluids identifies hyperfucosylated lactosamines on the N-linked glycans of overexpressed glycoproteins CTRC gene polymorphism (p.G60=; c.180 C > T) in acute pancreatitis.Pathogenic cellular role of the p.L104P human cationic trypsinogen variant in chronic pancreatitis Functional effects of 13 rare PRSS1 variants presumed to cause chronic pancreatitis.Genetic risk factors for pancreatic disorders.Tighter Control by Chymotrypsin C (CTRC) Explains Lack of Association between Human Anionic Trypsinogen and Hereditary Pancreatitis.Autoactivation of mouse trypsinogens is regulated by chymotrypsin C via cleavage of the autolysis loop.Clinical and Genetic Risk Factors for Acute Pancreatitis in Patients With Acute Lymphoblastic Leukemia.Molecular basis for pancreatitis.Zymogen activation confers thermodynamic stability on a key peptide bond and protects human cationic trypsin from degradation.Human cationic trypsinogen (PRSS1) variants and chronic pancreatitis.Human trypsinogens in the pancreas and in cancer.Association of CTRC and SPINK1 gene variants with recurrent hospitalizations for pancreatitis or acute abdominal pain in lipoprotein lipase deficiency Proteomic analysis of zymogen granules.Genetics of pancreatitis: a guide for clinicians.Genetics of acute and chronic pancreatitis.Identification of a functional enhancer variant within the chronic pancreatitis-associated SPINK1 c.101A>G (p.Asn34Ser)-containing haplotype.Complex Formation of Human Proelastases with Procarboxypeptidases A1 and A2.Asparagine-linked glycosylation of human chymotrypsin C is required for folding and secretion but not for enzyme activity.

P2860

Q24620760-78814A2C-4A2D-4594-9DAB-DA65F74AED3B Q24645261-6CD303A1-7DF6-4781-BFE2-E7B086AEA0BB Q24650338-1E31CF4B-07BF-4FFF-B14B-1F571D2A9CE1 Q26775406-C5321863-EDC8-4FD3-A78A-2034ADB7DF0B Q26801332-AC9E3906-AD34-494F-A915-54705F0656E3 Q27000406-2EE2D8FC-4B3F-4C82-8D71-4CA1CB23F664 Q27003930-965C5529-7D9E-4F6E-A3E8-4CD209C849FB Q27676497-E00ED3EC-2283-4C1E-BC82-2FA95CB81C42 Q27693296-0BF74660-D39A-4257-9CCC-5E9526C98221 Q30000783-F8F0C661-341F-4CBB-94E1-47239BB57202 Q33764920-9EB3808C-14CE-4F37-853B-6D200BACF179 Q33843764-A82C0B23-028B-4B91-B579-6A89A1D7F32D Q33880616-3F742C28-E0EA-4733-93C9-9E774BF092B2 Q34503091-FE82D4D6-0265-43A2-8F7F-602E942DE55B Q34508844-4C825C19-04F7-49D3-89D0-700EFAB555C3 Q34667122-81041E9F-7B3C-48A9-A590-ACB5B3D291F7 Q35181335-CC2B675F-8B08-42B3-979F-3815795811AD Q35212921-04392650-6342-4206-8829-F0696D72AE91 Q35565390-9ADE1840-EBCA-445A-BDBD-DAEA7B2AB6F0 Q35837145-3282B5C9-F19C-4812-8DA6-B6A427A8DE2C Q36016998-6E9306ED-3060-4576-9DAC-F77D4862B8CC Q36089872-30F539B2-E88E-4B00-96AC-4D777A06DC7A Q36251687-69CBA58C-DFD8-40FE-ACC3-73FFC8EA4301 Q36775826-3F89FB08-BC0B-4DAD-B6DA-634288580D86 Q36927073-7644095E-4651-450E-A4F2-66F87ACD7F3D Q36933359-E9128544-E6BA-4758-B432-06C45F5FF409 Q37065823-99CB7005-A192-4B6A-8F2E-AFC8CBBE478C Q37099760-112D67A4-8843-4F88-BDFC-4B47B60B4F71 Q37130123-78DB851D-D3BD-4393-AC5C-C1D0EDE1443F Q37362100-8ACFB5F6-8595-4706-A6A7-DCF1265F5690 Q37596314-50726D4D-A718-4F86-859C-D13304AFF7FF Q37629167-F5572B63-C123-4FA8-9E74-F4AE6308C3A5 Q37693897-DFB49399-B3C2-4ABC-B42D-67E42B5B30FE Q37725572-B48574FA-8D69-4021-82A2-5A8472904176 Q37802876-F396F12E-6A8C-43F0-83BB-96900EB1BF95 Q37869759-D1915F5F-9DB6-4D40-87B6-039EAEBB024F Q38122993-CBD12008-4921-4FAE-80C9-FFC95546732A Q38757404-41E10E8F-0F35-4CA5-A047-8428D568AE80 Q38760758-CC39CCD1-870F-4E9A-AED3-C735C1BDC947 Q38963298-C6AB378A-CBD0-47A9-BF8D-42FB04BC9FD6

P2860

Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: identity with Rinderknecht's enzyme Y

http://www.wikidata.org/entity/Q24675338

description

2007 nî lūn-bûn

@nan

2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

Chymotrypsin C (caldecrin) pro ...... y with Rinderknecht's enzyme Y

@ast

Chymotrypsin C (caldecrin) pro ...... y with Rinderknecht's enzyme Y

@en

Chymotrypsin C (caldecrin) pro ...... y with Rinderknecht's enzyme Y

@nl

type

label

Chymotrypsin C (caldecrin) pro ...... y with Rinderknecht's enzyme Y

@ast

Chymotrypsin C (caldecrin) pro ...... y with Rinderknecht's enzyme Y

@en

Chymotrypsin C (caldecrin) pro ...... y with Rinderknecht's enzyme Y

@nl

prefLabel

Chymotrypsin C (caldecrin) pro ...... y with Rinderknecht's enzyme Y

@ast

Chymotrypsin C (caldecrin) pro ...... y with Rinderknecht's enzyme Y

@en

Chymotrypsin C (caldecrin) pro ...... y with Rinderknecht's enzyme Y

@nl

P1433

Q24675338-EA959106-68C9-43EF-86B8-86392D7BEC06

P1476

Q24675338-D01EE73D-AFD3-48CC-8DD8-2DE43A298813

P2093

Q24675338-2492563E-93A3-487F-AE61-D80CE4C662DD

P2860

Q24675338-131E0885-D2EB-4C21-A5EB-84EF6B50541B

Q24675338-1D042E26-CD3C-4ABC-BFCF-010DFC29F88E

Q24675338-202394BB-5A89-44E0-9F46-C7E0A98B62D2

Q24675338-289F8563-C0F9-4DA2-9833-575791643E0A

Q24675338-36A0AD48-3632-405F-BEB7-FC35C6A50986

Q24675338-42C37A74-9C79-4CB4-8154-6DE707C02D56

Q24675338-4D47DE64-C161-4A4F-84C5-E2B0544D276A

Q24675338-4D6FDF1F-76F2-47C8-A767-EDFF4F023EDF

Q24675338-5CD75D1D-BD27-479B-8880-FCAC7509D221

Q24675338-5D4049FF-7469-4B52-B161-6B9F6CC32964

P304

Q24675338-89F3F746-DD44-433D-AEFE-2F6C8E96AD0E

P31

Q24675338-C1EB60A0-ED0A-4058-9ECF-CEBD77B9A2FE

P356

Q24675338-30C57114-437E-4C8B-A28F-6F17B91DEF97

P407

Q24675338-AE8D072A-CCD0-45D5-B704-4C79B9DA48E1

P433

Q24675338-DB97DF39-15F1-42E8-BE90-354CC30AD640

P478

Q24675338-818BF91D-57D9-462D-B467-436F997C72DF

P50

Q24675338-6A0AB95A-91FE-4EBC-9538-19F972297586

P577

Q24675338-BF76DD1C-49F4-45DA-AA19-60BDC2688EBA

P5875

Q24675338-F58B13D1-4500-4901-ABF9-6DC82226162A

P698

Q24675338-C1B9BC7F-8D1A-4B53-9A1F-174FAB26AC48

P932

Q24675338-969863E9-7322-4E12-B56A-F118CDB3B028

P356

PNAS.0703714104

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Chymotrypsin C (caldecrin) pro ...... y with Rinderknecht's enzyme Y

@en

P2093

Richárd Szmola

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

P2860

Human anionic trypsinogen: properties of autocatalytic activation and degradation and implications in pancreatic diseases

Mesotrypsin: a new inhibitor-resistant protease from a zymogen in human pancreatic tissue and fluid

Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene

Mutations of human cationic trypsinogen (PRSS1) and chronic pancreatitis

Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151

Structural determinants of the half-life and cleavage site preference in the autolytic inactivation of chymotrypsin

Activation of trypsinogen in large endocytic vacuoles of pancreatic acinar cells.

Studies of intestinal digestion and absorption in the human.

Characterization of human exocrine pancreatic proteins by two-dimensional isoelectric focusing/sodium dodecyl sulfate gel electrophoresis.

Trypsinogen variants in pancreatic juice of healthy volunteers, chronic alcoholics, and patients with pancreatitis and cancer of the pancreas

P304

11227-11232

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

P31

scholarly article

P356

10.1073/PNAS.0703714104

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

P407

P433

27

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

P478

104

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

P50

Miklós Sahin-Tóth

P577

2007-06-25T00:00:00Z

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

P5875

6245581

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

P698

17592142

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

P932

2040881

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