Results 271 to 280 of about 23,206 (306)
Biomaterials‐Involved Construction of Extracellular Matrices for Tumor Blockade Therapy
Extracellular matrices (ECMs) play a crucial role in tumor growth and metastases by providing structural support and facilitating tumor cell proliferation. In this review, we explore the development of artificial ECMs engineered through biomineralization, fibrogenesis, and gelation. These bioinspired ECMs create a protective barrier around tumor cells,
Jinfeng Sun+4 more
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Schematic illustration of structural and functional biomimicry. The upper part shows BP with various structures such as monolayered, surface‐microstructural, bilayered and multilayered. The bottom part exhibits BP with different functions including immune regulation, drugs/cells/factors/ions loading, as well as bioelectrical stimulation and ...
Yuhan Du+7 more
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This review examines how multiphase systems address the limitations of bio‐based and biodegradable polymers. It also discusses the application of various bio‐based polymers in developing these systems, highlighting their potential for sustainable food packaging solutions. ABSTRACT In recent decades, the thermoplastics market has experienced significant
Almas Mustafa+7 more
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Structural Units in Collagen Fibrils [PDF]
THE structure of fibrous proteins has long been a subject of controversy. X-ray and electron microscope evidence has accumulated which suggests that single chains may not run the whole length of the fibril, but that the latter is made up of an aggregation of smaller parts of quite definite size.
Pauline M. Cowan+2 more
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Crystalline regions in collagen fibrils
Journal of Molecular Biology, 1985A new image processing technique, content-dependent anisotropic spatial frequency filtering, has been developed to visualize the location and orientation of crystalline regions in collagen fibril cross-sections. The results show that most crystalline regions are oriented with their approximately 4 nm periodicity directed radially from the fibril centre.
Hulmes, Dj, Holmes, Df, Cummings, C.
openaire +5 more sources
Physica A: Statistical Mechanics and its Applications, 1997
Abstract While simple aggregation in solution typically leads to ramified objects, some polymers and proteins form filamentous structures. The aggregation of collagen, a structural protein, from monomers to fibrils was studied by light scattering and atomic force microscopy.
I. Yadegari+5 more
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Abstract While simple aggregation in solution typically leads to ramified objects, some polymers and proteins form filamentous structures. The aggregation of collagen, a structural protein, from monomers to fibrils was studied by light scattering and atomic force microscopy.
I. Yadegari+5 more
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Collagen Fibrils in Nanophthalmic Sclerae
Japanese Journal of Ophthalmology, 2001To examine collagen fibrils in 3 nanophthalmos sclerae and to compare them with normal control sclerae morphometrically.Three cases of nanophthalmos associated with uveal effusion were studied. When sclerectomy was performed, scleral specimens were collected and fixed with 3% glutaraldehyde/2.5% paraformaldehyde.
Haruki Abe+2 more
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Special form of collagen fibrils [PDF]
We found a special form of collagen fibrils in tentorium cerebelli and internal cranial periost of hen with two characteristics under electron-microscope: 1. Collagen fibrils showing branching and anastomosing somewhat like the branching and anastomosing of heart muscle fibers. 2.
Lu G, Peng Ql
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Collagen Fibril Structure in Lamprey
Journal of Molecular Biology, 1994X-ray diffraction and electron microscopy are used to compare the molecular and higher order structure of collagen fibrils in three tissues of the lamprey: the dermis, perinotochord and notochord sheath. These lamprey tissues are known to contain five distinct genetic types of fibrillar collagen.
Kathleen Cassidy Belbruno+3 more
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Stabilization of collagen fibrils by hydroxyproline
Biochemistry, 1986The substitution of hydroxyproline for proline in position Y of the repeating Gly-X-Y tripeptide sequence of collagen-like poly(tripeptide)s (i.e., in the position in which Hyp occurs naturally) is predicted to enhance the stability of aggregates of triple helices, while the substitution of Hyp in position X (where no Hyp occurs naturally) is predicted
George Nemethy, Harold A. Scheraga
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