-
5
-
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0025828716
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Collagens in the FACIT group: diverse molecular bridges in extracellular matrices
-
(1991)
Trends Biochem Sci
, vol.16
, pp. 191-194
-
-
Shaw1
Olsen2
-
10
-
-
0028245136
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Molecular genetics of chondrodysplasias, including clues to development, structure, and function
-
(1994)
Curr Opin Rheumatol
, vol.6
, pp. 345-350
-
-
Byers1
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13
-
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0020569249
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Embryonic lethal mutation in mice induced by retrovirus insertion into the alpha 1(I) collagen gene
-
(1983)
Nature
, vol.304
, pp. 315-320
-
-
Schnieke1
Harbers2
Jaenisch3
-
14
-
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0028246068
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Self-assembly of collagen I from a proband homozygous for a mutation that substituted serine for glycine at position 661 in the alpha 2(I) chain. Possible relationship between the effects of mutations on critical concentration and the severity of the phenotype
-
of special interest, In this continuation of studies on the phenotypic consequences of mutations in collagen I genes in osteogenesis imperfecta, the authors study fibrillogenesis in vitro with procollagen I from a patient who was homozygous for a Gly→Ser substitution in the α2(I) collagen chain. The self-assembly of mutant protein showed a greater lag period and a slower rate of propagation than normal collagen I. A comparison with previously studied mutations suggests a correlation between disease phenotype and the effect of mutations on the critical concentration of fibril assembly.
-
(1994)
J Biol Chem
, vol.269
, pp. 11614-11619
-
-
Romanic1
Spotila2
Adachi3
Engel4
Hojima5
Prockop6
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15
-
-
0028337485
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Substitution of an aspartic acid for glycine 700 in the alpha 2(I) chain of type I collagen in a recurrent lethal type II osteogenesis imperfecta dramatically affects the mineralization of bone
-
of special interest, A study of the effects on bone mineralization of a dominant collagen I mutation responsible for recurrent lethal osteogenesis imperfecta. The mutation, a Gly→Asp substitution in the α2(I) chain, caused intracellular retention of abnormal collagen, few and thin fibrils in bone matrix, and the presence of abnormal spheritic aggregates of mineral.
-
(1994)
J Biol Chem
, vol.269
, pp. 14751-14758
-
-
Cohen-Solal1
Zylberberg2
Sangalli3
Gomez Lira4
Mottes5
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16
-
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0028247036
-
Further evidence that the failure to cleave the aminopropeptide of type I procollagen is the cause of Ehlers—Danlos syndrome type VII
-
(1994)
Hum Mutat
, vol.3
, pp. 358-364
-
-
Ho1
Kong2
Kuffner3
Hsu4
Cheah5
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20
-
-
0028220202
-
Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta
-
of special interest, In this careful study, the kinetics of triple helix formation are measured for procollagen I from six patients with Gly→Cys substitutions at various positions along the proα1(I) collagen chain. The data demonstrate a correlation between melting temperature and delay in helix formation, and provides direct experimental evidence for a delay in the zipper-like folding of collagen molecules due to Gly substitutions along the triple-helical domain.
-
(1994)
J Mol Biol
, vol.236
, pp. 940-949
-
-
Raghunath1
Bruckner2
Steinmann3
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22
-
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0028025532
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Structural characteristics of crosslinking sites in type V collagen of bone. Chain specificities and heterotypic links to type I collagen
-
(1994)
Eur J Biochem
, vol.224
, pp. 943-950
-
-
Niyibizi1
Eyre2
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25
-
-
0028938776
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A COL2A1 mutation in achondrogenesis type II results in the replacement of type II collagen by type I and III collagens in cartilage
-
of special interest, A Gly→Ser substitution at position 769 of the α1(II) collagen chain is shown to lead to a total absence of collagen II in the cartilage of a 20 week old human fetus and a compensatory increase in collagens I and III. These collagens are unable to support a normal cartilage structure, but allow chondrocyte maturation to hypertrophy and collagen X production to take place.
-
(1995)
J Biol Chem
, vol.270
, pp. 1747-1753
-
-
Chan1
Cole2
Chow3
Mundlos4
Bateman5
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26
-
-
0025732094
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Expression of the mouse alpha 1(II) collagen gene is not restricted to cartilage during development
-
(1991)
Development
, vol.111
, pp. 945-953
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-
Cheah1
Lau2
Au3
Tam4
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28
-
-
84966163623
-
Targeted mutation in the col5a2 gene reveals a regulatory role for type V collagen during matrix assembly
-
of outstanding interest, Using a gene-targeting approach, the authors have eliminated the connecting peptide between the N-propeptide and the COL domain in murine α2(V) collagen. In homozygous mutant mice abnormalities are observed in the vertebral column, skin and cornea. In skin and cornea collagen I fibrils are disorganized and unusually thick. The study provides the first in vivo evidence for a role of collagen V in regulation of collagen fibril diameters and suggests that certain forms of Ehlers—Danlos syndrome may be due to mutations in genes encoding the subunits of collagen V.
-
(1995)
Nature Genet
, vol.9
, pp. 31-36
-
-
Andrikopoulos1
Liu2
Keene3
Jaenisch4
Ramirez5
-
29
-
-
0028815297
-
A fibrillar collagen gene, Col11a1, is essential for skeletal morphogenesis
-
of outstanding interest, The study demonstrates that a frameshift mutation in Col11a1 causes autosomal recessive chondrodysplasia (cho) in mice. Cartilage from homozygous mutants is extremely soft, contains atypical thick collagen fibrils, and does not retain the complexes of aggrecan, hyaluronan and link protein. A deficient maturation of chondrocytes to hypertrophy and a loss of columnar organization of cells in growth plates cause severe disproportionate dwarfism in homozygotes. The study provides the first in vivo evidence for a role of collagen XI in the regulation of fibril diameters, retention of proteoglycans, and maturation and spatial organization of chondrocytes.
-
(1995)
Cell
, vol.80
, pp. 423-430
-
-
Li1
Lacerda2
Warman3
Beier4
Yoshioka5
Ninomiya6
Oxford7
Morris8
Andrikopoulos9
Ramirez10
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31
-
-
0028362351
-
Integrating with integrins
-
of special interest, A review integrating a variety of studies to support the thesis that signalling by integrins provides a mechanism for interaction of signals in response to adhesion, soluble hormones and mechanical forces.
-
(1994)
Mol Biol Cell
, vol.5
, pp. 389-393
-
-
Schwartz1
Ingber2
-
32
-
-
0028815298
-
Autosomal dominant and recessive osteochondrodysplasias associated with the COL11A2 locus
-
of outstanding interest, In this first identification of human genetic disorders caused by mutations in a ‘minor’ fibrillar collagen, the authors demonstrate that mutations in COL11A2 can cause both dominant and recessive Stickler-like syndromes without ocular involvement. The findings also suggest that weak mutations in collagen XI deserve further study as potential genetic risk factors for primary generalized osteoarthritis.
-
(1995)
Cell
, vol.80
, pp. 431-437
-
-
Vikkula1
Mariman2
Lui3
Zhidkova4
Tiller5
Goldbring6
Van Beersum7
Malefijt8
Van den Hoogen9
Ropers10
-
33
-
-
0028325987
-
Autoimmune response against the bullous pemphigoid 180 autoantigen
-
of special interest, An interesting study demonstrating that polyclonal antibodies raised in rabbits against epitopes in the extracellular portion of α1(XVII) collagen cause a subepidermal blistering disease resembling bullous pemphigoid when injected into neonatal mice.
-
(1994)
Dermatology
, vol.1
, pp. 34-37
-
-
Liu1
Diaz2
Giudice3
-
34
-
-
0028348553
-
Dominant dystrophic epidermolysis bullosa: identification of a Gly-->Ser substitution in the triple-helical domain of type VII collagen.
-
of special interest, The first demonstration that dominant dystrophic epidermolysis bullosa is caused by a mutation in the triple-helical domain of collagen VII, leading to the formation of abnormal anchoring fibrils.
-
(1994)
Proceedings of the National Academy of Sciences
, vol.91
, pp. 3549-3553
-
-
Christiano1
Ryynanen2
Uitto3
-
36
-
-
0028180153
-
Mutations in the alpha 2(IV) basement membrane collagen gene of Caenorhabditis elegans produce phenotypes of differing severities
-
of special interest, A continuation of studies on the effects of collagen mutations in C. elegans, this paper analyzes a large number of mutations in let-2 encoding α2(IV) collagen. Interallelic complementation patterns are interpreted on the basis of protein—protein interactions.
-
(1994)
EMBO J
, vol.13
, pp. 3278-3285
-
-
Sibley1
Graham2
Von Mende3
Kramer4
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37
-
-
0028171098
-
Collagen IV alpha 3, alpha 4, and alpha 5 chains in rodent basal laminae: sequence, distribution, association with laminins, and developmental switches
-
of special interest, This first systematic analysis of the tissue distribution of all collagen IV chains (except α6, IV)) in rodents provides the basis for further functional studies of the different collagen IV isoforms. During development of the glomerular basement membrane in the kidney a switch between α1(IV)/α2(IV) and α3(IV)/α5(IV) collagen is associated with a switch in laminin isotypes.
-
(1994)
J Cell Biol
, vol.127
, pp. 879-891
-
-
Miner1
Sanes2
-
40
-
-
0028353676
-
Deletions in the COL4A5 collagen gene in X-linked Alport syndrome. Characterization of the pathological transcripts in nonrenal cells and correlation with disease expression
-
of special interest, Identification of 14 different COL4A5 deletions in patients with juvenile-type X-linked Alport syndrome; in four patients with intragenic deletions, immunohistochemistry also demonstrated absence of α3(IV) in glomerular basement membranes. This suggests that the α3(IV) and α5(IV) chains are incorporated into the basement membrane in an interdependent fashion, perhaps as part of the same trimeric molecule.
-
(1994)
J Clin Invest
, vol.93
, pp. 1195-1207
-
-
Antignac1
Knebelmann2
Drouot3
Gros4
Deschenes5
HorsCayla6
Zhou7
Tryggvason8
Grunfeld9
Broyer10
Gubler11
-
41
-
-
0028168648
-
Identification of mutations in the alpha 3(IV) and alpha 4(IV) collagen genes in autosomal recessive Alport syndrome
-
of outstanding interest, This first identification of homozygous mutations in the COL4A3 and COL4A4 genes in affected individuals in four families with autosomal Alport syndrome demonstrates that α3(IV) and α4(IV) collagen chains are important for the structural integrity of the glomerular basement membrane.
-
(1994)
Nature Genet
, vol.8
, pp. 77-81
-
-
Mochizuki1
Lemmink2
Mariyama3
Antignac4
Gubler5
Pirson6
Verellen-Dumoulin7
Chan8
Schroder9
-
43
-
-
0028173801
-
The alpha 3 chain of type IV collagen induces autoimmune Goodpasture syndrome
-
of special interest, As part of a continuing series of papers on the molecular basis of Goodpasture syndrome, the authors demonstrate that the α3(IV) carboxy-terminal domain has a unique capacity to induce a Goodpasture-like autoimmune disease in rabbits.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 6201-6205
-
-
Kalluri1
Gattone2
Noelken3
Hudson4
-
46
-
-
0028290671
-
Mice lacking alpha 1 (IX) collagen develop noninflammatory degenerative joint disease.
-
of special interest, Mice homozygous for inactivated α1(IX) collagen alleles are normal at birth, but develop a non-inflammatory degenerative disease of articular cartilage after birth. The study suggests that mutations in collagen IX genes should be considered as candidates for mild chondrodysplasias with early onset osteoarthritis in humans.
-
(1994)
Proceedings of the National Academy of Sciences
, vol.91
, pp. 5070-5074
-
-
Faessler1
Schnegelsberg2
Dausman3
Muragaki4
Shinya5
McCarthy6
Olsen7
Jaenisch8
-
49
-
-
0027971943
-
Type XII and XIV collagens mediate interactions between banded collagen fibers in vitro and may modulate extracellular matrix deformability.
-
of special interest, An interesting study demonstrating that the amino-terminal non-triple-helical regions of collagens XII and XIV promote gel contraction mediated by fibroblasts in collagen I gels. The effect, which is dose-dependent and inhibited by denaturation and specific antisera, suggests that collagens XII/XIV may modulate biomechanical properties of fibrillar collagen scaffolds.
-
(1994)
J Biol Chem
, vol.269
, pp. 28193-28199
-
-
Nishiyama1
McDonough2
Bruns3
Burgeson4
-
52
-
-
0027488970
-
Spondylometaphyseal dysplasia in mice carrying a dominant negative mutation in a matrix protein specific for cartilage-to-bone transition
-
(1993)
Nature
, vol.365
, pp. 56-61
-
-
Jacenko1
LuValle2
Olsen3
-
54
-
-
0028965555
-
Type X collagen multimer assembly in vitro is prevented by a Gly618 to Val mutation in the α1(X) NC1 domain resulting in Schmid metaphyseal chondrodysplasia
-
of special interest, An in vitro assay of collagen X multimer assembly demonstrates that a mutation identified in Schmid metaphyseal chondrodysplasia prevents assembly. The result is consistent with previous suggestions that collagen X mutations in this disorder are haploinsufficiency mutations.
-
(1995)
J Biol Chem
, vol.270
, pp. 4558-4562
-
-
Chan1
Cole2
Rogers3
Bateman4
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