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Colchicine and microfibril orientation [PDF]
Protoplasma, 1976 Investigations on the mechanism of orientation of the cellulose microfibrils of the green algaOocystis solitaria have been carried out. This organism demonstrates easily observable and highly ordered microfibrils in its wall, which are arranged parallel to one another and regularly alternate at 90‡ from layer to layer of which there are approximately ...
David Robinson, H. Sachs, I. Grimm
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Biomacromolecules, 2006
Never-dried native celluloses (bleached sulfite wood pulp, cotton, tunicin, and bacterial cellulose) were disintegrated into individual microfibrils after oxidation mediated by the 2,2,6,6-tetramethylpiperidine-1-oxyl (TEMPO) radical followed by a ...
Tsuguyuki Saito +4 more
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Never-dried native celluloses (bleached sulfite wood pulp, cotton, tunicin, and bacterial cellulose) were disintegrated into individual microfibrils after oxidation mediated by the 2,2,6,6-tetramethylpiperidine-1-oxyl (TEMPO) radical followed by a ...
Tsuguyuki Saito +4 more
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Microfibrils in the myotendon junctions
Cells Tissues Organs, 1978Myotendon junctions in the rectus abdominis muscles of bull frogs were examined by the fixation combination of tannic acid and glutaraldehyde using electron microscopy. The features observed on myotendon junctions were the following: (1) There were many deep invaginations of muscle cell membrane at the end of the muscle fibers.
Seiichiro Inokuchi +3 more
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2005
Fibrillin microfibrils are widely distributed extracellular matrix assemblies that endow elastic and nonelastic connective tissues with long-range elasticity. They direct tropoelastin deposition during elastic fibrillogenesis and form an outer mantle for mature elastic fibers.
Kielty, Cay M. +3 more
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Fibrillin microfibrils are widely distributed extracellular matrix assemblies that endow elastic and nonelastic connective tissues with long-range elasticity. They direct tropoelastin deposition during elastic fibrillogenesis and form an outer mantle for mature elastic fibers.
Kielty, Cay M. +3 more
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Structure and packing of microfibrils in collagen
Journal of Molecular Biology, 1973Abstract X-ray diffraction, patterns suggest that the five-stranded microfibrils in the collagen of rat tail tendon are supercoiled and packed together on a square lattice with a statistical distribution of axial displacements between nearest neighbours.
Andrew Miller, D.A.D. Parry
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Biochemical Journal, 2016
The 10-12 nm diameter microfibrils of the extracellular matrix (ECM) impart both structural and regulatory properties to load-bearing connective tissues.
S. Jensen, P. Handford
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The 10-12 nm diameter microfibrils of the extracellular matrix (ECM) impart both structural and regulatory properties to load-bearing connective tissues.
S. Jensen, P. Handford
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Microtubules and Microfibrils in Human Platelets
Thrombosis and Haemostasis, 1966SummaryThe microtubules and microfibrils of human platelets are described. They are studied under conditions that give as little alterations as possible. Conclusions on their localisation in vivo are drawn and their possible role in maintaining the platelet shape is discussed.
Molenaar I, Sixma Jj
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2010
Microfibrils are supramolecular structures ubiquitously found in the extracellular matrix of elastic and nonelastic tissues. The three members of the cysteine-rich fibrillin family constitute the core of microfibrils. Mutations in fibrillin-1 and -2 lead to a number of heritable connective tissue disorders termed fibrillinopathies.
Dieter P. Reinhardt, Dirk Hubmacher
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Microfibrils are supramolecular structures ubiquitously found in the extracellular matrix of elastic and nonelastic tissues. The three members of the cysteine-rich fibrillin family constitute the core of microfibrils. Mutations in fibrillin-1 and -2 lead to a number of heritable connective tissue disorders termed fibrillinopathies.
Dieter P. Reinhardt, Dirk Hubmacher
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Packing of microfibrils in collagen
Journal of Molecular Biology, 1974Abstract X-ray diffraction data obtained from rat tail tendon can be indexed on a tetragonal unit cell with a = 2 × 38·47 A , c = 4 × 670 A , space group P41 or P43, in which all the intermicrofibril contacts are quasi-equivalent.
Andrew Miller +2 more
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Structure of the α-keratin microfibril
Journal of Molecular Biology, 1976The fine detail in the X-ray diffraction pattern of α-keratin has been explored out to spacings of 4 A by a direct mapping of the cylindrically averagedintensity transform. The meridional maxima lie on a set of layer lines corresponding to an axially projected repeat of structure of 470 A, and the distribution of nonmeridional maxima is consistent with
T.P. MacRae, E. Suzuki, R.D.B. Fraser
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