Defective secretion of recombinant fragments of fibrillin-1: implications of protein misfolding for the pathogenesis of Marfan syndrome and related disorders.

Defective secretion of recombinant fragments of fibrillin-1: implications of protein misfolding for the pathogenesis of Marfan syndrome and related disorders.

Fibrillin-1 is a large modular glycoprotein that assembles to form 10-12 nm microfibrils in the extracellular matrix. Mutations in the fibrillin-1 gene (FBN1) cause Marfan syndrome and related connective tissue disorders (fibrillinopathies) that show autosomal dominant inheritance. The pathogenic me...

Bibliografske podrobnosti
Main Authors:	Whiteman, P, Handford, P
Format:	Journal article
Jezik:	English
Izdano:	2003

Podobne knjige/članki

Fibrillin-1 misfolding and disease.
od: Whiteman, P, et al.
Izdano: (2006)

Cellular and molecular studies of Marfan syndrome mutations identify co-operative protein folding in the cbEGF12-13 region of fibrillin-1.
od: Whiteman, P, et al.
Izdano: (2007)

Investigating molecular mechanisms underlying Marfan syndrome, based on fibrillin-1 secretion and assembly
od: Atwa, O
Izdano: (2020)

Cooperative Mechanism of ADAMTS/ ADAMTSL and Fibrillin-1 in the Marfan Syndrome and Acromelic Dysplasias
od: Pauline Arnaud, et al.
Izdano: (2021-11-01)

Fibrillin-1, a calcium binding protein of extracellular matrix.
od: Handford, P
Izdano: (2000)

Insights into fibrillin-1 structure and function from domain studies
od: Handford, P
Izdano: (2004)

Molecular pathology of the Marfan syndrome
od: Handford, P
Izdano: (1999)

Fibrillin-integrin interactions in health and disease.
od: Jovanović, J, et al.
Izdano: (2008)

Fibrillin-integrin interactions in health and disease
od: Jovanovic, J, et al.
Izdano: (2008)

Fibrillin: from domain structure to supramolecular assembly.
od: Handford, P, et al.
Izdano: (2000)

Dissecting the fibrillin microfibril: structural insights into organization and function.
od: Jensen, SA, et al.
Izdano: (2012)

Molecular analysis of nine mutations in Fibrillin-l
od: Halliday, D, et al.
Izdano: (1999)

Cross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseases.
od: Rodrigo Morales, et al.
Izdano: (2013-09-01)

The molecular genetics of Marfan syndrome and related disorders.
od: Robinson, P, et al.
Izdano: (2006)

Structure of the integrin binding fragment from fibrillin-1 gives new insights into microfibril organization.
od: Lee, S, et al.
Izdano: (2004)

TB domain proteins: evolutionary insights into the multifaceted roles of fibrillins and LTBPs.
od: Robertson, I, et al.
Izdano: (2011)

Familial spontaneous pneumothorax is not linked to FBN-1, the defective gene in the Marfan syndrome.
od: Maskell, N, et al.
Izdano: (2000)

Ca2+-dependent interface formation in fibrillin-1.
od: Jensen, SA, et al.
Izdano: (2005)

Mutations in fibrillin-1 cause congenital scleroderma: stiff skin syndrome.
od: Loeys, B, et al.
Izdano: (2010)

Solution structure and dynamics of a calcium binding epidermal growth factor-like domain pair from the neonatal region of human fibrillin-1.
od: Smallridge, R, et al.
Izdano: (2003)

Dynamic analysis of fibrillin organization and function during avian development
od: Rongish, B, et al.
Izdano: (2004)

Targeted deletion of fibrillin-1 in the mouse eye results in ectopia lentis and other ocular phenotypes associated with Marfan syndrome
od: Wendell Jones, et al.
Izdano: (2019-01-01)

A G1127S change in calcium-binding epidermal growth factor-like domain 13 of human fibrillin-1 causes short range conformational effects.
od: Whiteman, P, et al.
Izdano: (2001)

Circulating fibrillin fragment concentrations in patients with and without aortic pathology
od: Eric J. Carlson, PhD, et al.
Izdano: (2022-01-01)

¹H, ¹³C and ¹⁵N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment.
od: Robertson, I, et al.
Izdano: (2014)

Molecular effects of homocysteine on cbEGF disulphide bonding: insights into the pathogenesis of homocystinuria and its clinical similarity to Marfan syndrome
od: Hutchinson, S, et al.
Izdano: (2004)

Neonatal Marfan syndrome: a case report of a novel fibrillin 1 mutation, with genotype-phenotype correlation and brief review of the literature
od: Flaminia Pugnaloni, et al.
Izdano: (2024-09-01)

Fibrillin-1 mutation contributes to Marfan syndrome by inhibiting Cav1.2-mediated cell proliferation in vascular smooth muscle cells
od: Wenfeng Lin, et al.
Izdano: (2023-12-01)

Structural consequences of cysteine substitutions C1977Y and C1977R in calcium-binding epidermal growth factor-like domain 30 of human fibrillin-1.
od: Suk, J, et al.
Izdano: (2004)

¹H, ¹³C and ¹⁵N assignments of the four N-terminal domains of human fibrillin-1.
od: Yadin, D, et al.
Izdano: (2014)

Characterisation of fibrillin-1 cDNA clones in a human fibroblast cell line that assembles microfibrils.
od: Kettle, S, et al.
Izdano: (2000)

Protein Misfolding in Pregnancy: Current Insights, Potential Mechanisms, and Implications for the Pathogenesis of Preeclampsia
od: Bani Medegan Fagla, et al.
Izdano: (2024-01-01)

Calcium binding to fibrillin-1 TB-cbEGF domain pairs: new insights into microfibril organisation
od: Jensen, SA, et al.
Izdano: (2004)

Twelve novel FBN1 mutations in Marfan syndrome and Marfan related phenotypes test the feasibility of FBN1 mutation testing in clinical practice.
od: Halliday, D, et al.
Izdano: (2002)

Structure and interdomain interactions of a hybrid domain: a disulphide-rich module of the fibrillin/LTBP superfamily of matrix proteins.
od: Jensen, SA, et al.
Izdano: (2009)

Molecular effects of calcium binding mutations in Marfan syndrome depend on domain context.
od: McGettrick, A, et al.
Izdano: (2000)

The evolution of extracellular fibrillins and their functional domains.
od: Adam Piha-Gossack, et al.
Izdano: (2012-01-01)

The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1.
od: Robertson, IB, et al.
Izdano: (2017)

Marfan and Marfan-like syndromes
od: J. De Backer, et al.
Izdano: (2009-03-01)

Microenvironmental regulation by fibrillin-1.
od: Gerhard Sengle, et al.
Izdano: (2012-01-01)