about
Conformational changes in the nuclear lamina induced by herpes simplex virus type 1 require genes U(L)31 and U(L)34Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processesMandibuloacral dysplasia is caused by a mutation in LMNA-encoding lamin A/CA novel homozygous p.Arg527Leu LMNA mutation in two unrelated Egyptian families causes overlapping mandibuloacral dysplasia and progeria syndromeSevere mandibuloacral dysplasia-associated lipodystrophy and progeria in a young girl with a novel homozygous Arg527Cys LMNA mutationAltered protein dynamics of disease-associated lamin A mutantsStructure of the lamin A/C R482W mutant responsible for dominant familial partial lipodystrophy (FPLD)Atomic structure of the vimentin central -helical domain and its implications for intermediate filament assemblyCrystal structures of the coil 2B fragment and the globular tail domain of human lamin B1Structural basis for heteromeric assembly and perinuclear organization of keratin filamentsImplications and Assessment of the Elastic Behavior of Lamins in LaminopathiesOrder and disorder in intermediate filament proteinsRegulation of lamin properties and functions: does phosphorylation do it all?Life at the edge: the nuclear envelope and human diseaseLaminopathies and the long strange trip from basic cell biology to therapyMonoclonal antibodies specific for disease-associated point-mutants: lamin A/C R453W and R482WEvolution of the lamin protein family: what introns can tell.SUMO regulates the assembly and function of a cytoplasmic intermediate filament protein in C. elegansDiseases of the nuclear envelope.LMNA Sequences of 60,706 Unrelated Individuals Reveal 132 Novel Missense Variants in A-Type Lamins and Suggest a Link between Variant p.G602S and Type 2 DiabetesFunctions and dysfunctions of the nuclear lamin Ig-fold domain in nuclear assembly, growth, and Emery-Dreifuss muscular dystrophy.Nuclear lamins.The lamin protein family."Laminopathies": a wide spectrum of human diseases.Inner nuclear membrane proteins: impact on human disease.Prelamin A, Zmpste24, misshapen cell nuclei, and progeria--new evidence suggesting that protein farnesylation could be important for disease pathogenesis.Direct actin binding to A- and B-type lamin tails and actin filament bundling by the lamin A tail.The nucleoporin Nup88 is interacting with nuclear lamin A.Nuclear lamins: major factors in the structural organization and function of the nucleus and chromatinNuclear lamins and chromatin: when structure meets function.Mutations in LMNA modulate the lamin A--Nesprin-2 interaction and cause LINC complex alterationsNuclear envelope proteins and neuromuscular diseases.Systematic identification of pathological lamin A interactors.LMNA cardiomyopathy: cell biology and genetics meet clinical medicine.Subcellular localization of SREBP1 depends on its interaction with the C-terminal region of wild-type and disease related A-type laminsMislocalization of prelamin A Tyr646Phe mutant to the nuclear pore complex in human embryonic kidney 293 cells.The nuclear envelope and human disease.Nuclear membrane diversity: underlying tissue-specific pathologies in disease?A-type lamins: guardians of the soma?Lamins at a glance.
P2860
Q24292954-FCEF9965-2357-4E57-94EC-DDB720B47DC2Q24319820-B3EE40F9-410D-4266-A3AE-BB22ECB63E73Q24612380-130A5EA2-5211-4959-AFDA-DA30F61D5CC9Q24627210-03AD6FB0-09CC-4613-B474-AEDE39540772Q24648917-0B80928C-8F75-4E85-A6A2-065F68C96A23Q24791233-73F8BE68-F22E-41A4-B49D-1484039F40D4Q27646419-14D77CDB-22FF-43F7-BA46-F6723CE70C3EQ27671298-46A3E56F-828A-4F20-861D-9264D875995AQ27676828-E844212E-9379-499B-AADF-A43CE444325FQ27681198-DC0C9226-7F25-4697-8E3B-725FE26693FDQ28078956-B6775E96-A8C2-499C-8B5C-0BC2D45A5F9DQ28081207-1417F41F-5445-422D-9F87-CCB3CDB58F6BQ28083281-0387FD4C-A570-491E-958D-A16527ECEECAQ28216767-AE1AE483-96DC-43AB-9FFD-E63C926B7A04Q28251294-06C056CC-71E3-4818-9D63-AA2E5A8E0E61Q28752198-52DEBB1D-FEF3-413C-BABC-FC96D9D1C166Q30410501-14269B6A-A727-4EEF-B575-596AB4583F69Q30492693-A163216E-11D4-40FB-A3FA-98DAA9B62E34Q33687043-17F1B5FE-8E1E-4444-9682-AD12A64011CEQ33799816-16BEA6FC-059F-4371-8DE8-C9B40C64CFA4Q34081419-E51D0231-ADD9-41F9-B78A-1244F9D9A156Q34136884-7DEFF8FB-5895-47DF-9D36-C22FD0F6BBA2Q34189692-EA03AAFB-5E8A-4EFB-9CCF-969BB15CCD56Q34242119-F2E2870F-C510-4FD6-8011-D4BED0ADAB77Q34252203-C0E5BF72-EA66-462F-87FD-CA3C7F0BF1D8Q34457223-A60323DB-49D4-4AAF-B7A9-76A2142E8645Q34521501-B9F71D2B-6C3D-49E8-B230-E6D188CD5D4AQ34749215-6C67966B-CEA0-4339-9413-DEFC53F67A20Q34766646-54E2CCC7-E0E8-4131-BBB4-31AEFD3F0DC0Q34925545-BEF71863-9680-4FC2-957B-998F33B7C223Q34972521-75B742F0-2A18-4514-BDF8-0FDF4422CC5DQ35093315-CEEC2E0C-0DE5-41C1-9665-5D4F66CD595FQ35119345-CBE5733F-DAC8-468F-B155-AB3E6FB50371Q35232610-F01A3B17-666C-47EC-962C-121B5CCE9FF8Q35549134-6FC230BE-2A5A-46E2-8BF0-568DF5E772D3Q35748457-3B935B51-79D3-4BC5-B04E-A4BDDE77AEEFQ35894422-41DADA0D-B3FB-467E-A1DA-72680D3BA195Q35909029-9512DE4A-36F4-45B6-8559-FF22AD6FA74DQ35934217-16924BE0-C377-40AF-8163-DFBEC51C6484Q36010368-ECDC8697-8683-4DC2-B68B-B3A16EED13F3
P2860
description
2002 nî lūn-bûn
@nan
2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մայիսին 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
Structure of the globular tail of nuclear lamin
@ast
Structure of the globular tail of nuclear lamin
@en
Structure of the globular tail of nuclear lamin
@nl
type
label
Structure of the globular tail of nuclear lamin
@ast
Structure of the globular tail of nuclear lamin
@en
Structure of the globular tail of nuclear lamin
@nl
prefLabel
Structure of the globular tail of nuclear lamin
@ast
Structure of the globular tail of nuclear lamin
@en
Structure of the globular tail of nuclear lamin
@nl
P2093
P2860
P3181
P356
P1476
Structure of the globular tail of nuclear lamin
@en
P2093
Eric D Werner
Steven E Shoelson
Young-In Chi
P2860
P304
P3181
P356
10.1074/JBC.C200038200
P407
P577
2002-05-17T00:00:00Z