A Contour Algorithm for Computing Stable Fiber Bundles of Nonautonomous, Noninvertible Maps

2016 ◽  
Vol 15 (2) ◽  
pp. 923-951 ◽  
Author(s):  
Thorsten Hüls
Keyword(s):  
Fiber Bundles ◽  
Noninvertible Maps

Dupuytren's Contracture and Microvessels

1981 ◽  
Vol 39 ◽  
pp. 470-471
Author(s):  
C. W. Klscher ◽  
D. Speer
Keyword(s):  
Hypertrophic Scar ◽  
Active Form ◽  
Scar Tissue ◽  
Vascular Supply ◽  
Fiber Bundles ◽  
Dupuytren’S Contracture ◽  
Palmar Fascia ◽  
Immune Disease ◽  
Dupuytren's Contracture ◽  
Longitudinal Fiber

Dupuytren's Contracture is a nodular proliferation of the longitudinal fiber bundles of palmar fascia with its attendant contraction. The factors attributed to its etiology have included trauma, diabetes, alcoholism, arthritis, and auto-immune disease. The tissue has been observed by electron microscopy and found to contain myofibroblasts.Dupuytren's Contracture constitutes a scar, and as such, excessive collagen can be observed, along with an active form of fibroblast.Previous studies of the hypertrophic scar have led us to propose that integral in the initiation and sustenance of scar tissue is a profusion of microvascular regeneration, much of which becomes and remains occluded producing a hypoxia which stimulates fibroblast synthesis. Thus, when considering a study of Dupuytren's Contracture, we predicted finding occluded microvessels at or near the fascial scarring focus.Three cases of Dupuytren's Contracture yielded similar specimens, which were fixed in Karnovskys fluid for 2 to 20 days. Upon removal of the contracture bands care was taken to include the contiguous fatty and areolar tissue which contain the vascular supply and to identify the junctional area between old and new fascia.

Ultrastructural Features of the Oral Apparatus of Stentor

1976 ◽  
Vol 34 ◽  
pp. 142-143
Author(s):  
Elizabeth F. Howell
Keyword(s):  
Plasma Membrane ◽  
Osmium Tetroxide ◽  
Buccal Cavity ◽  
Fiber Bundles ◽  
Microtubular Root ◽  
Stentor Coeruleus ◽  
Root Fiber

The ultrastructure of the normal oral apparatus of Stentor has not been extensively studied. I report here on the ultrastructure of the buccal cavity of Stentor coeruleus.Stentor coeruleus was fixed in either a buffered mixture of osmium tetroxide and glutaraldehyde, or in buffered glutaraldehyde alone. Cells were then dehydrated and embedded in a mixture of Epon and Araldite.An extensive adoral zone of membranelles surrounds the anterior of the cell, and each membranelle consists of 2 parallel rows of cilia. These extend down into the buccal cavity. Two microtubular root fibers, or nemadesmata (Figs. 2 and 5), extend deeply into the cytoplasm from the base of each ciliary kinetosome. Mitochondria are usually closely associated with the root fiber bundles, and small vesicles are present between the nemadesmata of adjacent kinetosomes (Fig. 5). In the cytopharyngeal, non-ciliated areas of the buccal cavity, microtubular ribbons which extend into the cytoplasm are aligned perpendicular to the plasma membrane of the buccal cavity (Figs. 1 and 2).

Microstructures of SiC and Si3N4 with fibrous inclusions

1986 ◽  
Vol 44 ◽  
pp. 492-493
Author(s):  
N. J. Tighe ◽  
J. Sun ◽  
R.-M. Hu
Keyword(s):  
Vapor Deposition ◽  
Chemical Vapor ◽  
Crack Deflection ◽  
Fiber Bundles ◽  
High Temperature Strength ◽  
Graphite Fiber ◽  
Triple Junctions ◽  
Transmission Electron ◽  
Compact Graphite ◽  
Deposition Techniques

Particles of BN,and C are added in amounts of 1 to 40% to SiC and Si3N4 ceramics in order to improve their mechanical properties. The ceramics are then processed by sintering, hot-pressing and chemical vapor deposition techniques to produce dense products. Crack deflection at the particles can increase toughness. However the high temperature strength and toughness are determined byphase interactions in the environmental conditions used for testing. Examination of the ceramics by transmission electron microscopy has shown that the carbon and boron nitride particles have a fibrous texture. In the sintered aSiC ceramic the carbon appears as graphite fiber bundles in the triple junctions and as compact graphite particles within some grains. Examples of these inclusions are shown in Fig. 1A and B.

Hybrid Chalcogenide/Polymer Coherent Fiber Bundles for MWIR Image Relays

2021 ◽  
Author(s):  
Cesar Lopez-Zelaya ◽  
Li Zhang ◽  
Anthony Badillo ◽  
Felix Tan ◽  
Joshua Kaufman ◽  
...  
Keyword(s):  
Fiber Bundles

The Use of Optical Fiber Bundles Combined with Electrochemistry for Chemical Imaging

ChemPhysChem ◽  
2003 ◽  
Vol 4 (2) ◽  
pp. 186-192 ◽  
Author(s):  
Sabine Szunerits ◽  
David R. Walt
Keyword(s):  
Optical Fiber ◽  
Chemical Imaging ◽  
Fiber Bundles

Strengths of ceramic fiber bundles: Theory and practice

2017 ◽  
Vol 100 (11) ◽  
pp. 5306-5317 ◽  
Author(s):  
Evan B. Callaway ◽  
Frank W. Zok
Keyword(s):  
Theory And Practice ◽  
Ceramic Fiber ◽  
Fiber Bundles

Caffeine alters cardiac myofilament activity and regulation independently of Ca2+ binding to troponin C

1995 ◽  
Vol 268 (6) ◽  
pp. C1348-C1353 ◽  
Author(s):  
F. M. Powers ◽  
R. J. Solaro
Keyword(s):  
Atpase Activity ◽  
Isometric Force ◽  
Troponin C ◽  
Fiber Bundles ◽  
Direct Effects ◽  
Skinned Fiber ◽  
Myofilament Function ◽  
Cardiac Myofilament ◽  
Myosin Interaction ◽  
Skinned Fiber Bundles

We investigated the mechanism by which caffeine influences myofilament responsiveness to Ca2+ by measuring isometric force, Ca2+ binding, and ATPase activity of dog cardiac myofilament proteins. Caffeine (20 mM) increased submaximal and depressed maximal force in skinned fiber bundles. Although the Ca2+ sensitivity of myofilament activity was increased by caffeine, there was no effect on Ca2+ binding to troponin C (TnC) in skinned fiber bundles. To determine if caffeine altered actin-myosin interaction or affected myosin directly, myofibrillar, actomyosin, and myosin ATPase activities were measured. Maximal Ca(2+)-activated myofibrillar Mg(2+)-ATPase activity was depressed by 20 mM caffeine, whereas submaximal Mg(2+)-ATPase activities were not changed. Actomyosin Mg(2+)-ATPase activity was significantly depressed by caffeine concentrations > or = 15 mM. Myosin Ca(2+)-ATPase activity was depressed by caffeine, whereas Mg(2+)-ATPase and K(EDTA)-ATPase activities were not affected. These data suggest that caffeine affects myofilament function via a mechanism that is independent of TnC-Ca2+ binding but that may involve direct effects on actin-cross-bridge interaction.

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