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Methods in Molecular Biology (Clifton, N.J.)
|
June 7, 2000
Electron cryomicroscopy of fibrillar collagens
R S Meadows, D F Holmes, C J Gilpin, et al.
Journal of Ultrastructure Research
|
April 1, 1985
Mica sandwich technique for preparing macromolecules for rotary shadowing
A P Mould, D F Holmes, K E Kadler, et al.
The Journal of Biological Chemistry
|
June 21, 1996
Assembly in vitro of thin and thick fibrils of collagen II from recombinant procollagen II. The monomers in the tips of thick fibrils have the opposite orientation from monomers in the growing tips of collagen I fibrils
A Fertala, D F Holmes, K E Kadler, et al.
Journal of Molecular Biology
|
May 26, 1998
Surface located procollagen N-propeptides on dermatosparactic collagen fibrils are not cleaved by procollagen N-proteinase and do not inhibit binding of decorin to the fibril surface
R B Watson, D F Holmes, H K Graham, et al.
The Biochemical Journal
|
April 15, 1985
Type X collagen, a product of hypertrophic chondrocytes
C M Kielty, A P Kwan, D F Holmes, et al.
The Journal of Cell Biology
|
February 10, 1997
Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
K G Danielson, H Baribault, D F Holmes, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
June 8, 2001
Corneal collagen fibril structure in three dimensions: Structural insights into fibril assembly, mechanical properties, and tissue organization
D F Holmes, C J Gilpin, C Baldock, et al.
The Journal of Biological Chemistry
|
May 5, 1992
Ehlers Danlos syndrome type VIIB. Incomplete cleavage of abnormal type I procollagen by N-proteinase in vitro results in the formation of copolymers of collagen and partially cleaved pNcollagen that are near circular in cross-section
R B Watson, G A Wallis, D F Holmes, et al.
Micron (Oxford, England : 1993)
|
September 28, 2000
Collagen fibril organisation in mammalian vitreous by freeze etch/rotary shadowing electron microscopy
K J Bos, D F Holmes, R S Meadows, et al.
The Journal of Biological Chemistry
|
December 15, 1992
Type I procollagens containing substitutions of aspartate, arginine, and cysteine for glycine in the pro alpha 1 (I) chain are cleaved slowly by N-proteinase, but only the cysteine substitution introduces a kink in the molecule
S J Lightfoot, D F Holmes, A Brass, et al.
Page
of 5
Search research articles
Search
Showing results (31-40 of 50) with videos related to
Sort By:
Page
of 5
Methods in Molecular Biology (Clifton, N.J.)
|
June 7, 2000
Electron cryomicroscopy of fibrillar collagens
R S Meadows, D F Holmes, C J Gilpin, et al.
Journal of Ultrastructure Research
|
April 1, 1985
Mica sandwich technique for preparing macromolecules for rotary shadowing
A P Mould, D F Holmes, K E Kadler, et al.
The Journal of Biological Chemistry
|
June 21, 1996
Assembly in vitro of thin and thick fibrils of collagen II from recombinant procollagen II. The monomers in the tips of thick fibrils have the opposite orientation from monomers in the growing tips of collagen I fibrils
A Fertala, D F Holmes, K E Kadler, et al.
Journal of Molecular Biology
|
May 26, 1998
Surface located procollagen N-propeptides on dermatosparactic collagen fibrils are not cleaved by procollagen N-proteinase and do not inhibit binding of decorin to the fibril surface
R B Watson, D F Holmes, H K Graham, et al.
The Biochemical Journal
|
April 15, 1985
Type X collagen, a product of hypertrophic chondrocytes
C M Kielty, A P Kwan, D F Holmes, et al.
The Journal of Cell Biology
|
February 10, 1997
Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
K G Danielson, H Baribault, D F Holmes, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
June 8, 2001
Corneal collagen fibril structure in three dimensions: Structural insights into fibril assembly, mechanical properties, and tissue organization
D F Holmes, C J Gilpin, C Baldock, et al.
The Journal of Biological Chemistry
|
May 5, 1992
Ehlers Danlos syndrome type VIIB. Incomplete cleavage of abnormal type I procollagen by N-proteinase in vitro results in the formation of copolymers of collagen and partially cleaved pNcollagen that are near circular in cross-section
R B Watson, G A Wallis, D F Holmes, et al.
Micron (Oxford, England : 1993)
|
September 28, 2000
Collagen fibril organisation in mammalian vitreous by freeze etch/rotary shadowing electron microscopy
K J Bos, D F Holmes, R S Meadows, et al.
The Journal of Biological Chemistry
|
December 15, 1992
Type I procollagens containing substitutions of aspartate, arginine, and cysteine for glycine in the pro alpha 1 (I) chain are cleaved slowly by N-proteinase, but only the cysteine substitution introduces a kink in the molecule
S J Lightfoot, D F Holmes, A Brass, et al.
Page
of 5