Structural and biophysical studies of PCSK9 and its mutants linked to familial hypercholesterolemia - Wikidata - thesis-toulmin - TriplyDB

Structural and biophysical studies of PCSK9 and its mutants linked to familial hypercholesterolemia

Structural and biophysical studies of PCSK9 and its mutants linked to familial hypercholesterolemia

http://www.wikidata.org/entity/Q27644461

about

Annexin A2 is a natural extrahepatic inhibitor of the PCSK9-induced LDL receptor degradation Mechanistic implications for LDL receptor degradation from the PCSK9/LDLR structure at neutral pH The proprotein convertase PCSK9 induces the degradation of low density lipoprotein receptor (LDLR) and its closest family members VLDLR and ApoER2 Self-association of human PCSK9 correlates with its LDLR-degrading activity Annexin A2 is a C-terminal PCSK9-binding protein that regulates endogenous low density lipoprotein receptor levels The PCSK9 decade New developments in atherosclerosis: clinical potential of PCSK9 inhibition Hypercholesterolemia, low density lipoprotein receptor and proprotein convertase subtilisin/kexin-type 9 Mechanisms and genetic determinants regulating sterol absorption, circulating LDL levels, and sterol elimination: implications for classification and disease risk Proprotein convertase subtilisin/kexin type 9: from the discovery to the development of new therapies for cardiovascular diseases Cholesterol: the good, the bad, and the ugly - therapeutic targets for the treatment of dyslipidemia Trafficking Dynamics of PCSK9-Induced LDLR Degradation: Focus on Human PCSK9 Mutations and C-Terminal Domain The self-inhibited structure of full-length PCSK9 at 1.9 A reveals structural homology with resistin within the C-terminal domain Molecular basis for LDL receptor recognition by PCSK9 Antagonism of Secreted PCSK9 Increases Low Density Lipoprotein Receptor Expression in HepG2 Cells A proprotein convertase subtilisin/kexin type 9 neutralizing antibody reduces serum cholesterol in mice and nonhuman primates Structural and functional analysis of the CspB protease required for Clostridium spore germination Structure of the Mycosin-1 Protease from the Mycobacterial ESX-1 Protein Type VII Secretion System Identification of a Small Peptide That Inhibits PCSK9 Protein Binding to the Low Density Lipoprotein Receptor New Era of Lipid-Lowering Drugs Dynamics of hepatic and intestinal cholesterol and bile acid pathways: The impact of the animal model of estrogen deficiency and exercise training PCSK9 (Proprotein convertase subtilisin/kexin type 9) inhibitors: past, present, and the future Structural requirements for PCSK9-mediated degradation of the low-density lipoprotein receptor Catalytic activity is not required for secreted PCSK9 to reduce low density lipoprotein receptors in HepG2 cells In vivo evidence that furin from hepatocytes inactivates PCSK9 The multifaceted proprotein convertases: their unique, redundant, complementary, and opposite functions A proprotein convertase subtilisin-like/kexin type 9 (PCSK9) C-terminal domain antibody antigen-binding fragment inhibits PCSK9 internalization and restores low density lipoprotein uptake.Physiological and therapeutic regulation of PCSK9 activity in cardiovascular disease.PCSK9 inhibitor access barriers-issues and recommendations: Improving the access process for patients, clinicians and payers.Molecular population genetics of PCSK9: a signature of recent positive selection.Fabs enable single particle cryoEM studies of small proteins Novel domain interaction regulates secretion of proprotein convertase subtilisin/kexin type 9 (PCSK9) protein.The proprotein convertase subtilisin/kexin type 9 (PCSK9) active site and cleavage sequence differentially regulate protein secretion from proteolysis.Living the PCSK9 adventure: from the identification of a new gene in familial hypercholesterolemia towards a potential new class of anticholesterol drugs.PCSK9 and LDLR degradation: regulatory mechanisms in circulation and in cells.Proprotein convertase subtilisin/kexin type 9 (PCSK9) in lipid metabolism, atherosclerosis and ischemic stroke.A cholesterol-lowering VLP vaccine that targets PCSK9 The proprotein convertase subtilisin/kexin type 9 gene E670G polymorphism and serum lipid levels in the Guangxi Bai Ku Yao and Han populations A two-step binding model of PCSK9 interaction with the low density lipoprotein receptor Peptide-based anti-PCSK9 vaccines - an approach for long-term LDLc management

P2860

Q24294486-89E497C2-2981-4868-8C70-E083A1383273 Q24297165-A2A75697-AB31-43DA-A456-7DC41E1E4929 Q24301411-12C3AAC9-79F4-4C36-8B16-0C143753A218 Q24306591-9517C5BF-570D-490B-8201-B2335DD06A82 Q24313575-60591CB2-9F5B-4EF5-9DA4-EC34CDC61AD4 Q24615397-E055421A-ED07-43DF-9A88-4E046F640D0D Q26783407-D3A324E9-1638-4061-BA3C-9EC704A10F4B Q26786549-5288F3C0-20A4-4535-983D-63235C25EF4D Q27003094-B43586C4-5BC1-48B3-8D5E-9FAE9E3B0A8C Q27009477-AB3AF395-3B7E-49C7-A7BF-06E5316C7E6A Q27013494-5C12CAC5-908C-489B-8FDB-6464FAA6AF9D Q27339783-AE5996FC-CDFB-4AE0-8647-1B91A7418AAB Q27647905-8B9B2C9B-0983-41C3-8689-9605A6DB121B Q27649779-EAACE32E-5114-4875-8C9A-0DD968845208 Q27653836-1635DD7B-7F3E-416A-8954-C867C7DD832D Q27655476-7A0D7FE8-63B4-47EC-A752-C11616B69E1B Q27676376-FD960B8B-DA58-4C63-8BB1-0F1003E68BD5 Q27677641-4DE86180-130A-491E-982A-793CE196EDB1 Q27680601-5C591D0D-5CB4-47F8-8780-D6D956625BF1 Q28072298-A71AA1EF-78F3-427A-B524-810CEA83369E Q28073180-591AE763-B115-4937-AAC6-EEBC4857C4BA Q28083595-32500CCC-3D95-40E7-B025-34089D044C54 Q28292154-9156AABA-66CF-496F-B15B-C666FA4251FE Q28304381-299F48DB-9DC2-4EA7-95A7-22E77E23854D Q28504537-F7408554-8EB9-43D5-86A5-E75139F4BCA9 Q30541820-DB85A8C1-A59B-4896-8047-1B6B20ACC41E Q33532964-AE951F6A-FF8D-4C2A-92EE-2B12CCCE12D4 Q33599961-FEC28FFF-8FA6-44DB-BE32-D09C1E384387 Q33625574-7CC0D9F7-9189-456C-8DCE-33D0C65BE49C Q33743727-1A393206-D838-4746-880F-B31C7D047379 Q34223995-36B81930-920E-43D7-82B2-0C25C1D49E77 Q34227474-0CFBC559-E8D1-4DC1-94A0-7155D74DE605 Q34355679-3A8C71C4-311E-41D3-A075-5E2D94828491 Q34430377-898C47ED-BE0F-45FF-B997-72260E782172 Q34433146-CAD44F8B-D71B-4091-AC71-7A6EE6A70283 Q34479132-66A668BA-D91C-49A1-8E57-CC23BE6D4210 Q34496015-3FD551FD-AAD1-4323-8E72-B0365A598F39 Q34559768-D3138001-1C5B-4FA9-90E2-CC770672B451 Q34568486-24C7EACF-4E0A-43BC-9069-5668AAD99AC3 Q34634698-9331E22F-7B12-48EC-9ADC-4F11441B41F9

P2860

Structural and biophysical studies of PCSK9 and its mutants linked to familial hypercholesterolemia

http://www.wikidata.org/entity/Q27644461

description

2007 nî lūn-bûn

@nan

2007 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年学术文章

@wuu

2007年学术文章

@zh-cn

2007年学术文章

@zh-hans

2007年学术文章

@zh-my

2007年学术文章

@zh-sg

2007年學術文章

@yue

name

Structural and biophysical stu ...... familial hypercholesterolemia

@ast

Structural and biophysical stu ...... familial hypercholesterolemia

@en

Structural and biophysical stu ...... familial hypercholesterolemia

@nl

type

label

Structural and biophysical stu ...... familial hypercholesterolemia

@ast

Structural and biophysical stu ...... familial hypercholesterolemia

@en

Structural and biophysical stu ...... familial hypercholesterolemia

@nl

prefLabel

Structural and biophysical stu ...... familial hypercholesterolemia

@ast

Structural and biophysical stu ...... familial hypercholesterolemia

@en

Structural and biophysical stu ...... familial hypercholesterolemia

@nl

P1433

Q27644461-5EE5CF4F-7408-4015-B9B7-035DBB5C9FBE

P1476

Q27644461-CAC87CE9-0B7F-4B2E-9BB3-E56FD25D23E7

P2093

Q27644461-0883432D-E16C-4408-A02B-9C6ECD359471

Q27644461-183126FD-8C1B-4763-9D03-C71E1EE45D77

Q27644461-1B6A8798-C604-4175-A91E-1DC03B3ED841

Q27644461-2DC67CAB-3337-4C98-83C0-A96BFBB46DC6

Q27644461-317B29B6-62AD-4F4E-8085-B164DB44B478

Q27644461-79B4EB43-A7C2-4C2B-82B9-1032FBC4C4CA

Q27644461-7C7ABC84-DB98-440B-8183-DAE1CD13B0D5

Q27644461-9DB86AF1-B4E5-4AB0-8848-A3D9E205146C

Q27644461-A03615FB-AD87-476C-BA73-C0053964C838

Q27644461-A3A2FE38-320B-443C-A206-DA875E79441C

P2860

Q27644461-0DFBC769-2030-4CFD-9405-C1292E5902A7

Q27644461-1119B4A0-5F82-4AF7-ADD7-7B319888B2F7

Q27644461-1796A189-2730-4280-8A59-42E2B0BBEACC

Q27644461-22D23C2D-13A7-461B-ACE1-407E525D41DB

Q27644461-32E1AF00-9AF6-4295-BDC2-C7E0BBD07E15

Q27644461-392D6CFD-DA15-4A4D-8BF2-A78826A71B1C

Q27644461-90D920A4-C9C1-4C1D-AFC8-797D6C0FEE20

Q27644461-A8752291-49F2-4B85-8269-6C340E7ABB4E

Q27644461-AC59F274-0708-4E1A-B3C7-52A395D5011D

Q27644461-B7668615-A4F5-4756-8D24-26CFA4F44F21

P2888

Q27644461-4F23E38B-DC1D-4BE5-BFBA-102DF1BDDCC2

P304

Q27644461-573A6BA2-CAC8-450E-9168-A94C8089F796

P31

Q27644461-ECF9D02D-C4E6-414F-B510-52A3F65320E0

P3181

Q27644461-A3319C2D-9B68-4528-9995-87A0B56D5EB9

P356

Q27644461-1BB947F5-E1A9-4C9A-8745-9AE203A3A66C

P433

Q27644461-64CCC24C-BD3B-41CA-B7A7-779B0E67C72C

P478

Q27644461-A11A9757-7760-4CD0-AAAD-EA124CA42EB1

P577

Q27644461-41384845-1AFD-4849-A868-990239899E9C

P5875

Q27644461-9B866BF6-97CB-4B7E-AA9D-D48C1973C55C

P6179

Q27644461-720B4094-A999-4854-B047-CA6A54E5E47C

P698

Q27644461-08474DF2-1599-40DB-A762-537D24172383

P921

Q27644461-34AD393E-EB51-4C15-A53C-1CFC7689B1A7

Q27644461-A0B139F3-F49E-494B-8D79-A6407C15F3DE

P3181

P356

P1433

Nature Structural & Molecular Biology

P1476

Structural and biophysical stu ...... familial hypercholesterolemia

@en

P2093

Alison H Varghese

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

Andrew P Seddon

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

David Cunningham

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

Dennis E Danley

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

Donghui Xia

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

Jeffrey S Culp

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

Julie L Hawkins

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

Katherine M McGrath

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

Kieran F Geoghegan

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

Kim J Stutzman-Engwall

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

P2860

The secretory proprotein convertase neural apoptosis-regulated convertase 1 (NARC-1): liver regeneration and neuronal differentiation

The proprotein convertase (PC) PCSK9 is inactivated by furin and/or PC5/6A: functional consequences of natural mutations and post-translational modifications

Functional characterization of Narc 1, a novel proteinase related to proteinase K

Secreted PCSK9 decreases the number of LDL receptors in hepatocytes and in livers of parabiotic mice

Molecular biology of PCSK9: its role in LDL metabolism

Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus

Structure of the LDL receptor extracellular domain at endosomal pH

2.4 A resolution crystal structure of the prototypical hormone-processing protease Kex2 in complex with an Ala-Lys-Arg boronic acid inhibitor

The crystal structure of the proprotein processing proteinase furin explains its stringent specificity

The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 A resolution

P2888

P304

413-9

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

P31

scholarly article

P3181

913417

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

P356

10.1038/NSMB1235

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

P433

5

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

P478

14

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

P577

2007-05-01T00:00:00Z

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

P5875

232759668

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

P6179

1035856633

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

P698

17435765

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

P921

hypercholesterolemia