Faculty Opinions recommendation of Insight into the degradation of type-I collagen fibrils by MMP-8.

2013 ◽  
Author(s):  
Gregg B Fields
Keyword(s):  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I ◽  
Insight Into

Insight into the Degradation of Type-I Collagen Fibrils by MMP-8

2013 ◽  
Vol 425 (10) ◽  
pp. 1815-1825 ◽  
Author(s):  
Kuojung G. Lu ◽  
Collin M. Stultz
Keyword(s):  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I ◽  
Insight Into

scholarly journals Thermal (In)Stability of Type I Collagen Fibrils

2009 ◽  
Vol 102 (4) ◽  
Author(s):  
S. G. Gevorkian ◽  
A. E. Allahverdyan ◽  
D. S. Gevorgyan ◽  
A. L. Simonian
Keyword(s):  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I

Detection of type I collagen fibrils formation and dissociation by a fluorescence method based on thioflavin T

2016 ◽  
Vol 92 ◽  
pp. 1175-1182 ◽  
Author(s):  
Meilian Zou ◽  
Huan Yang ◽  
Haibo Wang ◽  
Haiyin Wang ◽  
Juntao Zhang ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Collagen Fibrils ◽  
Fluorescence Method ◽  
Thioflavin T ◽  
Type I

scholarly journals Mechanical Properties of Native and Cross-linked Type I Collagen Fibrils

2008 ◽  
Vol 94 (6) ◽  
pp. 2204-2211 ◽  
Author(s):  
Lanti Yang ◽  
Kees O. van der Werf ◽  
Carel F.C. Fitié ◽  
Martin L. Bennink ◽  
Pieter J. Dijkstra ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I

The ultrastructure of type I collagen at nanoscale: large or small D-spacing distribution?

Nanoscale ◽  
2014 ◽  
Vol 6 (14) ◽  
pp. 8134-8139 ◽  
Author(s):  
Hai-Nan Su ◽  
Li-Yuan Ran ◽  
Zhi-Hua Chen ◽  
Qi-Long Qin ◽  
Mei Shi ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I ◽  
Spacing Distribution ◽  
Large Distribution

The large distribution ofD-spacing values of type I collagen fibrils was due to image drift during measurement, and theD-spacing values were nearly identical both within a single fibril bundle and in different fibril bundles, exhibiting only a narrow distribution of 2.5 nm.

scholarly journals Comparison of the Structural Characteristics of Native Collagen Fibrils Derived from Bovine Tendons Using Two Different Methods: Modified Acid-Solubilized and Pepsin-Aided Extraction

Materials ◽  
2020 ◽  
Vol 13 (2) ◽  
pp. 358 ◽  
Author(s):  
Haiyan Ju ◽  
Xiuying Liu ◽  
Gang Zhang ◽  
Dezheng Liu ◽  
Yongsheng Yang
Keyword(s):  
Type I Collagen ◽  
Structural Characteristics ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Dry Weight ◽  
Collagen Fibrils ◽  
Type I ◽  
X Ray Diffraction ◽  
Aggregation Structure ◽  
Native Collagen

Native collagen fibrils (CF) were successfully extracted from bovine tendons using two different methods: modified acid-solubilized extraction for A-CF and pepsin-aided method for P-CF. The yields of A-CF and P-CF were up to 64.91% (±1.07% SD) and 56.78% (±1.22% SD) (dry weight basis), respectively. The analyses of both amino acid composition and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) confirmed that A-CF and P-CF were type I collagen fibrils. Both A-CF and P-CF retained the intact crystallinity and integrity of type I collagen’s natural structure by FTIR spectra, circular dichroism spectroscopy (CD) and X-ray diffraction detection. The aggregation structures of A-CF and P-CF were displayed by UV–Vis. However, A-CF showed more intact aggregation structure than P-CF. Microstructure and D-periodicities of A-CF and P-CF were observed (SEM and TEM). The diameters of A-CF and P-CF are about 386 and 282 nm, respectively. Although both A-CF and P-CF were theoretically concordant with the Schmitt hypothesis, A-CF was of evener thickness and higher integrity in terms of aggregation structure than P-CF. Modified acid-solubilized method provides a potential non-enzyme alternative to extract native collagen fibrils with uniform thickness and integral aggregation structure.

scholarly journals Platelet Adhesion to Native Type I Collagen Fibrils

1998 ◽  
Vol 273 (8) ◽  
pp. 4338-4344 ◽  
Author(s):  
Takashi Nakamura ◽  
G. A. Jamieson ◽  
Minoru Okuma ◽  
Jun-ichi Kambayashi ◽  
Narendra N. Tandon
Keyword(s):  
Platelet Adhesion ◽  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I

Intrafibrillar Mineralization of Collagen using a Liquid-Phase Mineral Precursor

2003 ◽  
Vol 774 ◽  
Author(s):  
Matthew J. Olszta ◽  
Elliot P. Douglas ◽  
Laurie B. Gower
Keyword(s):  
Liquid Phase ◽  
Material Science ◽  
Type I Collagen ◽  
Collagen Matrix ◽  
Collagen Fibrils ◽  
Type I ◽  
Mineral Phase ◽  
Capillary Action ◽  
Acid Etch ◽  
Mineralized Collagen

AbstractIntrafibrillar mineralization of type-I collagen with hydroxyapatite (HA) is the basis of the complex biological composite known as bone, which from a material science perspective is a fascinating example of an interpenetrating bioceramic composite. Using a polymer-induced liquid-precursor (PILP) process, collagen substrates were highly infiltrated with a liquid-phase mineral precursor to calcium carbonate (CaCO3). At sections of partially mineralized collagen, banded mineral patterns were observed perpendicular to the collagen fibrils, while other fibrils were completely mineralized. An acid etch, used to preferentially remove superficial mineral, further revealed such banded patterns in fully mineralized samples. Removal of the collagen matrix with a dilute hypochlorite solution showed an interpenetrating mineral phase, with mineral disks that spanned the diameter of the pre-existing collagen fibrils, supporting our hypothesis that intrafibrillar mineralization can be achieved via capillary action applied to a liquid-phase mineral precursor.

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