C. Ostlund

发表

Diseases of the nuclear envelope.

H. Worman, C. Ostlund, Yuexia Wang, 2010, Cold Spring Harbor perspectives in biology.

Both lamin A and lamin C mutations cause lamina instability as well as loss of internal nuclear lamin organization.

J. Broers, H. Kuijpers, F. Ramaekers, 2005, Experimental cell research.

Lamin-associated proteins.

H. Worman, C. Ostlund, 2004, Methods in cell biology.

Expression of lamin A mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with Dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy.

C. Vigouroux, B. Buendia, J. Capeau, 2003, Experimental cell research.

Autoantibodies in human chronic graft-versus-host disease after hematopoietic cell transplantation.

M. Manns, K. Tsuneyama, A. Ahmed, 1999, Clinical immunology.

Intracellular trafficking of emerin, the Emery-Dreifuss muscular dystrophy protein.

J. Lippincott-Schwartz, J. Ellenberg, E. Hallberg, 1999, Journal of cell science.

The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup100.

I. Olsson, C. Ostlund, J. Berrez, 2007, Experimental cell research.

The carboxyl-terminal region common to lamins A and C contains a DNA binding domain.

S. Zinn-Justin, H. Worman, J. Courvalin, 2003, Biochemistry.

Properties of lamin A mutants found in Emery-Dreifuss muscular dystrophy, cardiomyopathy and Dunnigan-type partial lipodystrophy.

H. Worman, K. Schwartz, G. Bonne, 2001, Journal of cell science.

The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy.

S. Zinn-Justin, B. Gilquin, J. Mornon, 2002, Structure.

Dependence of diffusional mobility of integral inner nuclear membrane proteins on A-type lamins.

C. Stewart, H. Worman, C. Ostlund, 2006, Biochemistry.

Intracellular trafficking and dynamics of double homeodomain proteins.

H. Worman, A. Belayew, C. Ostlund, 2005, Biochemistry.

Subcellular localization of SREBP1 depends on its interaction with the C-terminal region of wild-type and disease related A-type lamins.

B. Buendia, P. Roussel, S. Zinn-Justin, 2011, Experimental cell research.

Reduction of a 4q35-encoded nuclear envelope protein in muscle differentiation.

E. C. Schirmer, H. Worman, A. Hays, 2009, Biochemical and biophysical research communications.

Diseases of the nuclear envelope.

H. Worman, C. Ostlund, Yuexia Wang, 2010, Cold Spring Harbor perspectives in biology.