Literature DB >> 2415378

The nuclear lamins. A multigene family of proteins in evolution and differentiation.

G Krohne, R Benavente.   

Abstract

The nuclear lamina consists of a proteinaceous layer or meshwork situated subjacent to the inner nuclear membrane. It is a karyoskeletal structure formed by a polymer containing one to three major polypeptides collectively termed the lamins. In all cells examined of vertebrates and invertebrates, the lamins exhibit very similar Mr ranging from 60 000 to 80 000. In vertebrates, two groups of lamins can be distinguished by their isoelectric value, one being near-neutral and the other acidic (isoelectric pH values of 5.6 and lower). The lamins represent a family of polypeptides with regions highly conserved during evolution. In certain species, e.g., the amphibian, Xenopus laevis, they exhibit cell type-specific expression during embryonic development, terminal differentiation of certain somatic cells, and gametogenesis. The nuclear lamina of diverse cell types can be composed of one, two or three different lamin polypeptides, without obvious differences in its morphology.

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Year:  1986        PMID: 2415378     DOI: 10.1016/0014-4827(86)90421-0

Source DB:  PubMed          Journal:  Exp Cell Res        ISSN: 0014-4827            Impact factor:   3.905


  50 in total

1.  Alteration of cytokeratin expression following transdermal lidocaine hydrochloride iontophoresis.

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2.  Meiotic lamin C2: the unique amino-terminal hexapeptide GNAEGR is essential for nuclear envelope association.

Authors:  M Alsheimer; E von Glasenapp; M Schnolzer; H Heid; R Benavente
Journal:  Proc Natl Acad Sci U S A       Date:  2000-11-21       Impact factor: 11.205

3.  A novel karyoskeletal protein: characterization of protein NO145, the major component of nucleolar cortical skeleton in Xenopus oocytes.

Authors:  S Kneissel; W W Franke; J G Gall; H Heid; S Reidenbach; M Schnölzer; H Spring; H Zentgraf; M S Schmidt-Zachmann
Journal:  Mol Biol Cell       Date:  2001-12       Impact factor: 4.138

4.  Biochemical and immunological characterization of pea nuclear intermediate filament proteins.

Authors:  Sonal S D Blumenthal; Gregory B Clark; Stanley J Roux
Journal:  Planta       Date:  2004-01-15       Impact factor: 4.116

Review 5.  Nuclear shape, mechanics, and mechanotransduction.

Authors:  Kris Noel Dahl; Alexandre J S Ribeiro; Jan Lammerding
Journal:  Circ Res       Date:  2008-06-06       Impact factor: 17.367

6.  Characterization of a second highly conserved B-type lamin present in cells previously thought to contain only a single B-type lamin.

Authors:  T H Höger; K Zatloukal; I Waizenegger; G Krohne
Journal:  Chromosoma       Date:  1990-10       Impact factor: 4.316

7.  Dynamic properties of meiosis-specific lamin C2 and its impact on nuclear envelope integrity.

Authors:  Daniel Jahn; Sabine Schramm; Ricardo Benavente; Manfred Alsheimer
Journal:  Nucleus       Date:  2010-03-15       Impact factor: 4.197

8.  A lamin B receptor in the nuclear envelope.

Authors:  H J Worman; J Yuan; G Blobel; S D Georgatos
Journal:  Proc Natl Acad Sci U S A       Date:  1988-11       Impact factor: 11.205

9.  cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins.

Authors:  D Z Fisher; N Chaudhary; G Blobel
Journal:  Proc Natl Acad Sci U S A       Date:  1986-09       Impact factor: 11.205

10.  Nuclear A-type lamins are differentially expressed in human lung cancer subtypes.

Authors:  J L Broers; Y Raymond; M K Rot; H Kuijpers; S S Wagenaar; F C Ramaekers
Journal:  Am J Pathol       Date:  1993-07       Impact factor: 4.307

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