Prelamin A endoproteolytic processing in vitro by recombinant Zmpste24 - Wikidata - wikimedia - TriplyDB

Prelamin A endoproteolytic processing in vitro by recombinant Zmpste24

Prelamin A endoproteolytic processing in vitro by recombinant Zmpste24

http://www.wikidata.org/entity/Q40505214

about

The mutant form of lamin A that causes Hutchinson-Gilford progeria is a biomarker of cellular aging in human skin Mutational analysis of the ras converting enzyme reveals a requirement for glutamate and histidine residues Model of human aging: recent findings on Werner's and Hutchinson-Gilford progeria syndromes Ste24p Mediates Proteolysis of Both Isoprenylated and Non-prenylated Oligopeptides.Chemical inhibition of CaaX protease activity disrupts yeast Ras localization.Analysis of prelamin A biogenesis reveals the nucleus to be a CaaX processing compartment Regulation of lamin properties and functions: does phosphorylation do it all?Laminopathies and the long strange trip from basic cell biology to therapy Prelamin A farnesylation and progeroid syndromes Embryonic senescence and laminopathies in a progeroid zebrafish model Alterations in mitosis and cell cycle progression caused by a mutant lamin A known to accelerate human aging Farnesylation of lamin B1 is important for retention of nuclear chromatin during neuronal migration.Involvement of xeroderma pigmentosum group A (XPA) in progeria arising from defective maturation of prelamin A.Genomic instability and DNA damage responses in progeria arising from defective maturation of prelamin A.Dynamics of lamin-A processing following precursor accumulation.Diseases of the nuclear envelope.The posttranslational processing of prelamin A and disease.DNA damage and lamins Mechanobiology and the microcirculation: cellular, nuclear and fluid mechanics.Blocking protein farnesyltransferase improves nuclear blebbing in mouse fibroblasts with a targeted Hutchinson-Gilford progeria syndrome mutation.An accumulation of non-farnesylated prelamin A causes cardiomyopathy but not progeria.Blocking protein farnesyltransferase improves nuclear shape in fibroblasts from humans with progeroid syndromes Direct synthesis of lamin A, bypassing prelamin a processing, causes misshapen nuclei in fibroblasts but no detectable pathology in mice.Nuclear lamins and neurobiology.Inhibiting farnesylation reverses the nuclear morphology defect in a HeLa cell model for Hutchinson-Gilford progeria syndrome.DNA-damage accumulation and replicative arrest in Hutchinson-Gilford progeria syndrome Nuclear lamins.Functional coupling between the extracellular matrix and nuclear lamina by Wnt signaling in progeria.Requirements for efficient proteolytic cleavage of prelamin A by ZMPSTE24.The role of DNA damage in laminopathy progeroid syndromes.Inner nuclear membrane proteins: impact on human disease.Accelerated ageing in mice deficient in Zmpste24 protease is linked to p53 signalling activation.Prelamin A, Zmpste24, misshapen cell nuclei, and progeria--new evidence suggesting that protein farnesylation could be important for disease pathogenesis.The truncated prelamin A in Hutchinson-Gilford progeria syndrome alters segregation of A-type and B-type lamin homopolymers.HIV protease inhibitors do not cause the accumulation of prelamin A in PBMCs from patients receiving first line therapy: the ANRS EP45 "aging" study Lipid posttranslational modifications. Farnesyl transferase inhibitors.Nucleoplasmic lamins and their interaction partners, LAP2alpha, Rb, and BAF, in transcriptional regulation.Nuclear lamins: major factors in the structural organization and function of the nucleus and chromatin Nuclear lamins and chromatin: when structure meets function.Investigating the purpose of prelamin A processing

P2860

Q21144407-C6DEF95D-9888-4EAE-9B8C-65F376EBBE4C Q24611091-AFF219E2-0DEC-4600-BFB1-B3A6CC27191C Q24644033-7132C9E3-4AAE-4D2F-9853-E9EE2AB9543F Q27935867-48551AEC-7B95-41C7-9BDD-80FC4E88AAE4 Q27937343-16046729-1D68-44A6-A910-D44A1FFC5ECD Q27939423-EEC02C91-96F6-4AE3-A782-50E1ED962816 Q28083281-0E6E4211-0AE9-4775-9A6C-92F36526C315 Q28251294-25692F25-CCDA-4DA9-9AF6-6C0B821C43D9 Q28272957-6DB2CA63-4D41-4474-81F5-0B1BAFB98EA4 Q28477557-C36D9F11-A4EB-4E7E-9299-30AD0CC6CFE4 Q30479111-81618A41-FEA7-4CDA-9F23-08E3D8F030F3 Q30540136-DDF5A356-DDD9-4EBD-A0C8-E4BCE7DB8787 Q33298574-246238BA-56B5-46ED-8D60-F3A7A59D4D7B Q33511965-5A8CD28F-692D-4C0E-8C50-78CE0DA0116B Q33595869-4A23FA89-967A-4FA3-BE4D-C714A53AA367 Q33687043-6D15AA3C-7235-4AB0-A8FB-174B7963CC7E Q33758494-D833D622-4FF4-498F-A398-00EB90D7D1DC Q33844504-10C79672-D1DD-4872-B86A-32CC465C9EA9 Q33895715-9587D6A7-5407-4AE5-84A4-875894EE5912 Q33895774-6683A613-2816-47EC-AA4D-FCFB596F91CA Q33904465-813B9B5E-F470-4195-AD41-519E38C2962D Q33930224-2639B55E-4376-44DF-BE7D-7A3A6C5E0CC6 Q33966782-6685F37F-988F-46B6-95E4-06A60FD096F8 Q34056472-9E20D0C5-EE28-48C6-A51D-CD76610964F2 Q34063471-6C967F13-4C25-4296-88FD-7EF3017C2544 Q34079464-01535CA9-4B10-4A53-9BE8-A91621806763 Q34136884-7C59B930-C17D-44CA-982B-D139B95FF99A Q34137401-F526B634-199A-4B70-867B-8DA68840EB5E Q34166555-285A7D9B-D146-408D-A3DB-704059F9F9C1 Q34234762-ACC584F4-B7A3-48D8-B880-E74699B5B82C Q34252203-4BFD2726-8A0F-467E-8F5B-1B01A2471D0E Q34440150-AF1F1385-A797-4D3F-A05B-836524D3CFFE Q34457223-A9A46318-FE87-4723-90DD-4723C6190020 Q34494982-6521C522-6C23-4FE2-A26E-76CAC7C2E857 Q34534986-DD4AC467-237B-4989-B49D-56BFCFAAEC23 Q34651253-63B1823F-08FA-4FF3-A3B6-F0537DE1B6C6 Q34654052-5B208C32-C3C3-40FC-B5C0-DA6ABC4735EA Q34766646-5CA06B3F-D2A7-41B4-A502-F7DA673A4FBA Q34925545-533BFE1A-D1EF-4354-88FA-170D5D351445 Q35015891-221EF477-9730-48E5-8B17-6901F9A26B3A

P2860

Prelamin A endoproteolytic processing in vitro by recombinant Zmpste24

http://www.wikidata.org/entity/Q40505214

description

2005 nî lūn-bûn

@nan

2005年の論文

@ja

2005年学术文章

@wuu

2005年学术文章

@zh-cn

2005年学术文章

@zh-hans

2005年学术文章

@zh-my

2005年学术文章

@zh-sg

2005年學術文章

@yue

2005年學術文章

@zh

2005年學術文章

@zh-hant

name

Prelamin A endoproteolytic processing in vitro by recombinant Zmpste24

@en

type

label

Prelamin A endoproteolytic processing in vitro by recombinant Zmpste24

@en

prefLabel

Prelamin A endoproteolytic processing in vitro by recombinant Zmpste24

@en

P1433

Q40505214-39B6C38C-0D78-4B47-A804-25EB24DAB75D

P1476

Q40505214-9FB10387-3745-4B3F-B0EC-80A563DFACC0

P2093

Q40505214-0410115E-D1CF-402E-862B-2FB1B4A7107B

Q40505214-04876BFF-E5B4-497A-8634-4F7ED5570414

Q40505214-081F8795-63AB-4F89-98BD-65E05D56816E

Q40505214-2C9EC35D-9A10-44B5-A077-5E13197A1E36

Q40505214-79352FB2-50A1-4221-B1B2-C94249EB0BDC

Q40505214-DDC735D9-A275-4F0F-AEC3-D4DB5CD179AC

Q40505214-E8D10F65-60C6-42C3-A49F-4211C41F4242

P2860

Q40505214-048B855C-91DC-4B39-BD06-8D9461BA4DB5

Q40505214-0FAB63C8-4E82-41EB-B621-692CEA15C0EE

Q40505214-20EF448B-53DC-476D-B71D-0CE7D44BD13E

Q40505214-26B5CA68-BEDC-4D7C-B3B8-A94EC308AEF3

Q40505214-33185C4C-6919-46F7-A53D-9E0B69F0F78A

Q40505214-36E44597-86CE-4492-8087-5CB389DC556F

Q40505214-3D9B0396-7293-4E35-8E1B-FDB82BAC4F47

Q40505214-4503F16F-E70F-4A09-B004-6F47DFC78821

Q40505214-4CE56377-25D9-4E4B-A31B-8036CBC6BFEA

Q40505214-51248DBE-7762-4B6E-849F-7BDFC874BCCF

P304

Q40505214-7CBD3B74-611D-4BE1-9407-A023C0D0B456

P31

Q40505214-4767B434-9538-481E-B521-53829F4EA304

P356

Q40505214-61504777-E076-4BF8-9956-70E95331999B

P407

Q40505214-C6931DC0-419F-4207-9B3D-59AE13692E37

P433

Q40505214-69A00094-730E-4DFE-AE1B-27C9A33FE782

P478

Q40505214-13571819-9A5C-46C0-AFA8-B920521D5E3C

P577

Q40505214-924C78CF-1299-4E2A-905E-56B9A0386F50

P698

Q40505214-77D4E3F7-ED8A-426B-B2E0-CA7D921CAC52

P932

Q40505214-5BB0A5A4-3D5F-44C6-86C9-4AA97B2BBF6C

P356

P1433

Biochemical Journal

P1476

Prelamin A endoproteolytic processing in vitro by recombinant Zmpste24

@en

P2093

Antonio E Rusinol

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

Christine A Hrycyna

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

Danuta Kuszczak

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

Douglas P Corrigan

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

Douglas P Thewke

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

Michael S Sinensky

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

Susan Michaelis

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

P2860

Cloning and characterization of a mammalian prenyl protein-specific protease

Prenylated prelamin A interacts with Narf, a novel nuclear protein

Accumulation of mutant lamin A causes progressive changes in nuclear architecture in Hutchinson-Gilford progeria syndrome

Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processing

The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor.

Modulation of Ras and a-factor function by carboxyl-terminal proteolysis.

Zinc metalloproteinase, ZMPSTE24, is mutated in mandibuloacral dysplasia

Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome

The processing pathway of prelamin A

A novel membrane-associated metalloprotease, Ste24p, is required for the first step of NH2-terminal processing of the yeast a-factor precursor

P304

129-138

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

P31

scholarly article

P356

10.1042/BJ20041359

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

P407

P433

Pt 1

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

P478

387

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

P577

2005-04-01T00:00:00Z

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

P698

15479156

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

P932

1134940

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