Results 41 to 50 of about 23,678,950 (225)

Endothelial BMAL1 decline during aging leads to bone loss by destabilizing extracellular fibrillin-1. [PDF]

J Clin Invest
Yin Y, Tang Q, Yang J, Gui S, Zhang Y, Shen Y, Zhou X, Yu S, Chen G, Sun J, Han Z, Zhang L, Chen L.   +12 more
europepmc   +2 more sources

Fibrillin-1 Interactions with Heparin [PDF]

Journal of Biological Chemistry, 2005
Fibrillin-1 assembly into microfibrils and elastic fiber formation involves interactions with glycosaminoglycans. We have used BIAcore technology to investigate fibrillin-1 interactions with heparin and with heparin saccharides that are analogous to S-domains of heparan sulfate. We have identified four high affinity heparin-binding sites on fibrillin-1,
Stuart A. Cain, Clair Baldock, John T. Gallagher, Amanda Morgan, Daniel V. Bax, Anthony S. Weiss, C. Adrian Shuttleworth, Cay M. Kielty   +7 more
openalex   +5 more sources

Proteolysis of fibrillin-2 microfibrils is essential for normal skeletal development

eLife, 2022
The embryonic extracellular matrix (ECM) undergoes transition to mature ECM as development progresses, yet few mechanisms ensuring ECM proteostasis during this period are known.
Timothy J Mead, Daniel R Martin, Lauren W Wang, Stuart A Cain, Cagri Gulec, Elisabeth Cahill, Joseph Mauch, Dieter Reinhardt, Cecilia Lo, Clair Baldock, Suneel S Apte   +10 more
doaj   +1 more source

Characterization of metabolic health in mouse models of fibrillin-1 perturbation [PDF]

Matrix Biology, 2016
Clarissa S Craft, Lynn Y Sakai, Robert P Mecham   +2 more
exaly   +2 more sources

Is There a Relationship Between Pelvic Organ Prolapse and Tissue Fibrillin-1 Levels? [PDF]

International Neurourology Journal, 2015
Purpose: Pelvic organ prolapse is a multifactorial disorder in which extracellular matrix defects are implicated. Fibrillin-1 level is reduced in stress urinary incontinence.
Ayla Eser, Eylem Unlubilgin, Fatih Hizli, Muradiye Acar, Zeynep Kamalak, Aydin Kosus, Nermin Kosus, Deniz Hizli, Esra Gunduz   +8 more
doaj   +1 more source

Role of fibrilins in human cancer: A narrative review

Health Science Reports, 2023
Background Fibrillin is one of the extracellular matrix glycoproteins and participates in forming microfibrils found in many connective tissues. The microfibrils enable the elasticity and stretching properties of the ligaments and support connective ...
Mahsa Mahdizadehi, Marie Saghaeian Jazi, Seyyed Mostafa Mir, Seyyed Mehdi Jafari   +3 more
doaj   +1 more source

Fibrillin-1 regulates the bioavailability of TGFβ1 [PDF]

The Journal of Cell Biology, 2007
We have discovered that fibrillin-1, which forms extracellular microfibrils, can regulate the bioavailability of transforming growth factor (TGF) β1, a powerful cytokine that modulates cell survival and phenotype. Altered TGFβ signaling is a major contributor to the pathology of Marfan syndrome (MFS) and related diseases.
Cay M. Kielty, Cay M. Kielty, C. Adrian Shuttleworth, Stuart A. Cain, Sarah L. Dallas, Shazia S. Chaudhry, Shazia S. Chaudhry, Amanda Morgan   +7 more
openaire   +3 more sources

Pathogenic variants affecting the TB5 domain of the fibrillin-1 protein: not only in geleophysic/acromicric dysplasias but also in Marfan syndrome. [PDF]

J Med Genet
Arnaud P, Mougin Z, Baujat G, Drouin-Garraud V, El Chehadeh S, Gouya L, Odent S, Jondeau G, Boileau C, Hanna N, Le Goff C.   +10 more
europepmc   +3 more sources

Homotypic Fibrillin-1 Interactions in Microfibril Assembly [PDF]

Journal of Biological Chemistry, 2005
We have defined the homotypic interactions of fibrillin-1 to obtain new insights into microfibril assembly. Dose-dependent saturable high affinity binding was demonstrated between N-terminal fragments, between furin processed C-terminal fragments, and between these N- and C-terminal fragments.
Marson, Andrew, Rock, Matthew J., Cain, Stuart A., Freeman, Lyle J., Morgan, Amanda, Mellody, Kieran, Shuttleworth, C. Adrian, Baldock, Clair, Kielty, Cay M.   +8 more
openaire   +4 more sources

Processing of the Fibrillin-1 Carboxyl-terminal Domain [PDF]

Journal of Biological Chemistry, 1999
To investigate the processing and general properties of the fibrillin-1 carboxyl-terminal domain, three protein expression constructs have been developed as follows: one without the domain, one with the domain, and one with a mutation near the putative proteolytic processing site.
Dianna M. Milewicz, Timothy M. Ritty, Robert P. Mecham, Clarina Tisdale, Thomas J. Broekelmann   +4 more
openaire   +3 more sources