Results 111 to 120 of about 1,871 (159)

Characterisation of fibrillin-1 cDNA clones in a human fibroblast cell line that assembles microfibrils.

, 2000
Fibrillin-1 is a large extracellular glycoprotein which is a major structural component of 10-12 nm microfibrils. Defects in human fibrillin-1 give rise to the autosomal dominant connective tissue disease the Marfan syndrome and related disorders ...
Kettle, S, Sykes, B, Card, CM, Hutchinson, S, Handford, Penelope, Handford, PA   +5 more
core   +1 more source

A Clinicoimmunohistopathologic Study of Anetoderma: Is Protruding Type More Advanced in Stage Than Indented Type?

Journal of Immunology Research, 2016
Background. The clinical and histopathologic classification of anetoderma are not well characterized. Objective. We aimed to investigate the clinical and histopathologic characteristics of anetoderma and to correlate clinical phenotypes with ...
Jung Eun Kim, Ki Min Sohn, Young Jun Woo, Kwan Ho Jeong, Miri Kim, Jeong Deuk Lee, Jun Young Lee, Hyun Jeong Park, Gyong Moon Kim, Chul Jong Park, Dong Soo Yu, Hoon Kang   +11 more
doaj   +1 more source

P1148A in fibrillin-1 is not a mutation anymore [PDF]

Nature Genetics, 1997
M, Wang, K R, Mathews, K, Imaizumi, S, Beiraghi, B, Blumberg, M, Scheuner, J M, Graham, M, Godfrey   +7 more
openaire   +2 more sources

Expression of fibrillin-1 in focal nodular hyperplasia of the liver: a role in microcirculation adaptability.

, 2004
INTRODUCTION: It has been suggested that the elastic network plays an important role in the tissue response to mechanical stress. The components of the elastic network have been poorly studied in liver diseases.
Desmouliere, Alexis, Rosenbaum, Jean, Bioulac-Sage, Paulette, Alexis Desmouliere, Sébastien Lepreux, Paulette Bioulac-Sage, Balabaud, Charles, Charles Balabaud, Jean Rosenbaum, Lepreux, Sébastien   +9 more
core   +1 more source

The Biomechanics of Fibrillin Microfibrils: Lessons from the Ciliary Zonule

Cells
Marfan syndrome is an inherited connective tissue disorder that affects the cardiovascular, musculoskeletal, and ocular systems. It is caused by pathogenic variants in the fibrillin-1 gene (FBN1).
Pooja Rathaur, Juan Rodriguez, John Kuchtey, Samuel Insignares, Wendell B. Jones, Rachel W. Kuchtey, Steven Bassnett   +6 more
doaj   +1 more source

The Marfan syndrome genetics

Zdravniški Vestnik, 2005
Background: The Marfan syndrome is an autosomal dominant heritable disorder of connective tissue. It is caused by mutations in the fibrillin-1 gene encoding glycoprotein fibrillin-1, a component of microfibrils of extracellular matrix.
Galina Pungerčič
doaj  

Exploring thoracic aorta ECM alterations in Marfan syndrome: insights into aorta wall structure

Scientific Reports
Marfan syndrome is a connective tissue disorder caused by FBN1 mutations, leading to aortic wall fragility and increased susceptibility to aneurysm and dissection. This study investigated microstructural and molecular alterations in the thoracic aorta of
Rodrigo Barbosa de Souza, Luara Lucena Cassiano, Philipp Barnowski, Sara Ventura, Walter Miguel Turato, Suelen Cristina Russafa Nascimento, Giovanna Lodi Mignanelli, Waldir Caldeira, Ana Maria Cristina Rebelo Pinto da Fonseca Martins, Flavio de Carvalho Luposeli, Francisco Rafael Martins Laurindo, Dieter P. Reinhardt, Gerhard Sengle, Ivan Hong Jun Koh, Keith M. Meek, Philip N. Lewis   +15 more
doaj   +1 more source

Microfibril-associated glycoprotein-2 interacts with fibrillin-1 and fibrillin-2 suggesting a role for MAGP-2 in elastic fiber assembly

, 2002
Elastic fibers are composed of the protein elastin and a network of 10-12 nm microfibrils. The microfibrillar proteins include, among others, the fibrillins and microfibril-associated glycoproteins-1 and -2 (MAGP-1 and MAGP-2).
Kielty, Cay M., Michael Shipley, J., Penner, Akiyo S., Rock, Matthew J.   +3 more
core   +1 more source

Biochemical analyses of interactions among ADAMTSL proteins, fibrillin-1, and ADAMTS-10.

, 2012
(a) SPR sensorgrams showing binding of different concentrations of soluble ligands to the N-terminal half of fibrillin-1 (rF90), coupled onto a chip. Full-length ADAMTSL-2 (320-0 nM) interacts with rF90, as does the C-terminal end of ADAMTSL-3 (80-0 nM).
Susan J. Hayflick (189266), Eric J. Carlson (189254), Douglas R. Keene (46430), Mary K. Wirtz (189261), John H. Fessler (189265), Lynn Y. Sakai (189267), Ko Tsutsui (189248), Noe L. Charbonneau (189257), Gerhard Sengle (189245), Robert N. Ono (189259), Kiyotoshi Sekiguchi (106583), Liselotte I. Fessler (189264), Sara F. Tufa (189251), Takako Sasaki (142232), John R. Samples (189262)   +14 more
core   +1 more source

Expression of the fibrillin gene family in the development, differentiation and maintenance of mesenchyme cell types [PDF]

, 2015
Connective tissue initially arises from embryonic mesenchymal stem cells (MSC) that originate from the mesoderm during embryogenesis and are capable of differentiating into connective tissue lineages such as adipocytes, osteoblasts, chondrocytes and ...
Davis, Margaret Rose
core