Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a prelamin A processing defect. - Wikidata - awgldk - TriplyDB

Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a prelamin A processing defect.

Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a prelamin A processing defect.

http://www.wikidata.org/entity/Q34191451

about

Inhibiting farnesylation of progerin prevents the characteristic nuclear blebbing of Hutchinson-Gilford progeria syndrome Progeria: a rare genetic premature ageing disorder Lamin B1 is required for mouse development and nuclear integrity Targeting protein prenylation in progeria Mutational analysis of the ras converting enzyme reveals a requirement for glutamate and histidine residues Human ZMPSTE24 disease mutations: residual proteolytic activity correlates with disease severity Blocking protein farnesylation improves nuclear shape abnormalities in keratinocytes of mice expressing the prelamin A variant in Hutchinson-Gilford progeria syndrome Model of human aging: recent findings on Werner's and Hutchinson-Gilford progeria syndromes A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation Two faces of p53: aging and tumor suppression Hallmarks of progeroid syndromes: lessons from mice and reprogrammed cells Molecular insights into the premature aging disease progeria Mouse models of laminopathies The structural basis of ZMPSTE24-dependent laminopathies Analysis of prelamin A biogenesis reveals the nucleus to be a CaaX processing compartment Laminopathies and the long strange trip from basic cell biology to therapy Prelamin A farnesylation and progeroid syndromes Lamin A and ZMPSTE24 (FACE-1) defects cause nuclear disorganization and identify restrictive dermopathy as a lethal neonatal laminopathy Progeria of stem cells: stem cell exhaustion in Hutchinson-Gilford progeria syndrome Heterozygosity for Lmna deficiency eliminates the progeria-like phenotypes in Zmpste24-deficient mice ZMPSTE24 defends against influenza and other pathogenic viruses Acquisition of accurate data from intramolecular quenched fluorescence protease assays.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.Dynamics of lamin-A processing following precursor accumulation.Reciprocal knock-in mice to investigate the functional redundancy of lamin B1 and lamin B2.Nuclear localization signal deletion mutants of lamin A and progerin reveal insights into lamin A processing and emerin targeting Modulation of the inhibitor properties of dipeptidyl (acyloxy)methyl ketones toward the CaaX proteases.Diseases of the nuclear envelope.The posttranslational processing of prelamin A and disease.DNA damage and lamins 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 Therapeutic intervention based on protein prenylation and associated modifications 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.Insulin-like growth factor 1 treatment extends longevity in a mouse model of human premature aging by restoring somatotroph axis function.Functional coupling between the extracellular matrix and nuclear lamina by Wnt signaling in progeria.

P2860

Q24531946-A98CCE17-42DE-4DAF-99C8-0EEB8EE2561D Q24564144-7AAFBAAD-BBB3-4645-9D01-652F03FA9A95 Q24564213-BD710DB6-DDCC-4373-903F-690D4FFBE1C0 Q24594564-F046EEE1-21AE-417D-A981-8CCD76729CD3 Q24611091-20B345ED-93F2-490D-9FA0-9AC99C51A0DD Q24611268-FCF92BB3-BC29-4E4A-AF21-0D26E995E4C4 Q24627329-EC222C7A-3CA3-4321-8D89-3E17841E1516 Q24644033-BEE33CA8-1CC3-4B50-A471-33980144CAAA Q24671540-66A13539-C02F-4C0B-A9AE-EA201EBBD1D7 Q24681014-D600C1C1-14DE-4711-A3C1-79ADA3E02C17 Q26740026-C4ED70FD-00E3-4CC5-80AC-651F95CD5D88 Q26768972-545C7729-1195-4563-B307-9E896A60406E Q26829927-5A124B89-5D32-41F4-866C-E9BD757BA224 Q27684303-4820A698-33A0-4989-812F-D6D81A898DF7 Q27939423-10EAB7C5-56A7-4225-B670-47ADE93D6A0D Q28251294-2FBDA8E1-850F-4AEE-854D-4E22AEF2598E Q28272957-A861B3AD-6574-4262-9A92-57EB38D2B2F9 Q28277676-E2D51160-4027-4909-A629-7E9A4801C8E2 Q28288219-B17A04A4-297D-4E27-A9F5-54B4C8CFE05A Q28505849-C9445A9E-A7BA-497A-ACF1-D45B5B496987 Q29365364-05489378-41E5-44A1-925F-508613683FA0 Q30274929-F552A838-D4CD-4249-8EB8-E40567544B1F Q30479111-B36EB16C-FA39-4623-ADF6-471F6211871F Q30540136-4B732540-631B-41C8-93AD-555911B45BEE Q33595869-1BEEE89B-AA06-4AA5-A1D0-08902072A4D7 Q33604405-1AB2C1AD-81EE-4768-8B75-56ACC96697FB Q33638752-0F8A9F2A-31BF-4578-83F1-4F3D76E7B3E9 Q33653120-A1C0E374-A55E-4A45-812A-7E1192397A4B Q33687043-B8F91767-31BD-4D97-9639-1F521AF07D05 Q33758494-85230C89-AA92-45BA-AFDC-5AA895955619 Q33844504-77F6387E-F268-435E-8BA0-CC26828D4C70 Q33895774-D6F5220E-B7C5-417F-B6A5-1BAABE8C115C Q33904465-33AF0CD7-3CCC-4D31-97B0-D54BFBF5DB9A Q33930224-69F3C709-4FA9-4B7A-8F76-3109E799A8FF Q33943379-5F985FD4-7429-4D3C-ACFF-352F2DEA2D38 Q33966782-4E978489-BD48-4550-B444-B489C675BA60 Q34056472-60E6B19C-7717-4177-A041-92FE0BBAF1E0 Q34063471-F3A1B5F2-98AB-4B19-A204-1062D42E3FEF Q34136335-30F4FB36-A75F-4222-8E6E-54BAB7D544BA Q34137401-07FE365C-7724-4DBF-B876-821B94EFDADB

P2860

Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a prelamin A processing defect.

http://www.wikidata.org/entity/Q34191451

description

2002 nî lūn-bûn

@nan

2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Zmpste24 deficiency in mice ca ...... prelamin A processing defect.

@ast

Zmpste24 deficiency in mice ca ...... prelamin A processing defect.

@en

Zmpste24 deficiency in mice ca ...... prelamin A processing defect.

@nl

type

label

Zmpste24 deficiency in mice ca ...... prelamin A processing defect.

@ast

Zmpste24 deficiency in mice ca ...... prelamin A processing defect.

@en

Zmpste24 deficiency in mice ca ...... prelamin A processing defect.

@nl

prefLabel

Zmpste24 deficiency in mice ca ...... prelamin A processing defect.

@ast

Zmpste24 deficiency in mice ca ...... prelamin A processing defect.

@en

Zmpste24 deficiency in mice ca ...... prelamin A processing defect.

@nl

P1433

Q34191451-422FE3FC-E69D-4A00-88C3-5F26A1B43C90

P1476

Q34191451-2D93B2FA-2F1B-4B7D-824A-C1A4A3D6C054

P2093

Q34191451-01A278E9-6029-44B9-A885-B317DCD39F6C

Q34191451-17B14A0E-06B2-4785-9B1C-CB41FD9917C6

Q34191451-1DC051E4-DF2E-4E06-89CA-7C06FD6665BC

Q34191451-28B1AAA1-CFB0-4082-A255-6574BB7E2F20

Q34191451-361DD068-3BCA-4B08-878F-D84E266CA29B

Q34191451-40F6F5FD-22C1-4AC1-9220-4183D26380AB

Q34191451-4EBF077E-FFFB-4DA7-A491-EA726FCE5251

Q34191451-7E1AFBD7-D89F-4BBF-B458-7D0D5BC657E8

Q34191451-8FFB213E-2972-4733-8490-FA563468833D

Q34191451-AC47A049-9A62-453F-8C63-1AE3E905F4F7

P2860

Q34191451-05FD070B-A3D6-4AEC-A72D-FFEBF27665A0

Q34191451-0C9A9333-B22B-4DE5-90DC-006DDDDDF459

Q34191451-1288986E-4FB5-41F6-A2E6-950C5EF66D4A

Q34191451-2698DC93-8329-403F-86C8-78B933BA86B3

Q34191451-46B544A4-B59C-4E94-988F-1B0190410AA1

Q34191451-51B88046-B917-448D-8FEF-70427DAB17C9

Q34191451-561BD869-242B-4A07-9CAE-7DB7514CEDA7

Q34191451-5DD29E0C-D817-43D4-AB2F-6539359CF237

Q34191451-5F1863C2-DA05-4DDA-9FCD-31B4FD8637D6

Q34191451-773C66B3-AA25-4127-804D-1CA73DCD50C7

P304

Q34191451-075DD365-A389-4A41-85FC-E0FF5D665641

P31

Q34191451-C0409A09-4200-4788-B63C-98E5797E7DD7

P356

Q34191451-178E8FB8-55C7-45D2-BF62-A9638E397DE0

P407

Q34191451-2AE25A22-5735-48D8-A592-A8657753E1B3

P433

Q34191451-F6D1EB36-4208-4276-B68A-A026104D55F7

P478

Q34191451-B0C7FE6D-6403-46B6-ADF2-F10019CD8444

P50

Q34191451-C3389BE7-080F-40FA-91DA-4B97EF8840F2

P577

Q34191451-0411F643-9672-44B6-92AE-B1C9099408EB

P5875

Q34191451-6E706900-A01B-4287-B70B-891FFFF14213

P698

Q34191451-C9C4F954-E1C5-441A-AB61-15ECF783EA58

P932

Q34191451-B56B566A-8D8F-4C25-8056-B0E932901904

P356

P1433

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

P1476

Zmpste24 deficiency in mice ca ...... a prelamin A processing defect

@en

P2093

Andreas Mohr

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

Bryant Gavino

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

Christine Hong

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

Erik R Wisner

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

Harry Genant

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

Jed Ross

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

Lonnie V Kendall

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

Margarita Meta

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

Martin O Bergo

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

Nicholas Van Bruggen

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

P2860

Cloning and characterization of a mammalian prenyl protein-specific protease

Isoprenylcysteine carboxyl methyltransferase deficiency in mice

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

Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy

Transgenic mouse model of the mild dominant form of osteogenesis imperfecta

The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase that mediates C-terminal methylation of a-factor and RAS proteins.

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

Systematic genetic analysis with ordered arrays of yeast deletion mutants

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

Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells

P304

13049-13054

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

P31

scholarly article

P356

10.1073/PNAS.192460799

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

P407

P433

20

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

P478

99

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

P50

Stephen G. Young

P577

2002-09-16T00:00:00Z

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

P5875

11156046

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

P698

12235369

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

P932

130584

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