1,202 Citations
- M. RestR. GarroneD. Herbage
- 1993
Biology, Materials Science
- 37
- V. OttaniD. MartiniM. FranchiA. RuggeriM. Raspanti
- 2002
Biology, Materials Science
Micron
- 277
- S. Ricard-Blum
- 2011
Biology, Materials Science
Cold Spring Harbor perspectives in biology
The collagen family comprises 28 members that contain at least one triple-helical domain and plays structural roles and contribute to mechanical properties, organization, and shape of tissues.
- 1,617
- PDF
- Valentin WespLukas ScholzJanine M. Ziermann-CanabarroS. SchusterH. Stark
- 2024
Materials Science, Biology
bioRxiv
To increase the accuracy of collagen classification and prediction of their functions, the structure of these collagens and their expression in different tissues could result in a better focus on sequence segments of interest, and clusters with high interconnectivity can be found.
- PDF
- M. NoelkenB. Hudson
- 1995
Biology, Materials Science
- 2
- A. K. NicholasP. Jacques
- 2005
Materials Science, Biology
- E. AdachiI. HopkinsonI. HopkinsonToshihiko Hayashi
- 1997
Biology, Medicine
International review of cytology
- 128
- K. GelseaE. PöschlbT. Aignera
- 2003
Biology, Materials Science
The importance of different collagen types not only for the understanding of collagen-related diseases, but also as a basis for the therapeutical use of members of this protein family discussed in other chapters of this issue is indicated.
- 18
- PDF
- M. SutmullerJ. BruijnEmile de Heer
- 1997
Medicine, Biology
Histology and histopathology
The structure, function, and involvement in pathology of collagen types VII and X, a subgroup of non-fibrillar collagens, is discussed in this review.
- 62
- PDF
- Taina PihlajaniemiM. Rehn
- 1995
Biology
Progress in nucleic acid research and molecular…
- 118
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62 References
- B. BrodskyE. Eikenberry
- 1985
Materials Science
Annals of the New York Academy of Sciences
The current knowledge from X-ray diffraction work is summarized and some directions and ideas that may lead to a better understanding of how various connective tissues are constructed and maintained are indicated.
- 24
- P. BonaldoV. RussoF. BucciottiR. DolianaA. Colombatti
- 1990
Biology, Materials Science
Biochemistry
The type I collagen-binding and the cell-attachment properties of the alpha 3(VI) chain provide direct information for the role of type VI collagen in connective tissues.
- 257
- M. E. van der RestR. Garrone
- 1990
Biology, Materials Science
Biochimie
- 31
- R. FleischmajerJ. S. PerlishR. Timpl
- 1985
Biology, Medicine
Annals of the New York Academy of Sciences
The purpose of this study is to present additional data on the role of the aminopropeptide of type I and type I11 collagen during fibrillogenesis of embryonic and adult human skin and to discuss current hypotheses on the mechanism of collagen fibril formation.
- 112
- D. EyreStephen AponJiann-Jiu WuL. EricssonK. Walsh
- 1987
Biology, Materials Science
FEBS letters
- 238
- PDF
- G. VasiosIchiro NishimuraH. KonomiM. RestY. NinomiyaB. Olsen
- 1988
Biology, Materials Science
The Journal of biological chemistry
- 86
- PDF
- P. YurchencoJ. Schittny
- 1990
Biology, Materials Science
FASEB journal : official publication of the…
A large heparan sulfate proteoglycan, important for charge‐dependent molecular sieving, is firmly anchored in the basement membrane and can bind itself through a core‐protein interaction to form dimers and oligomers and bind laminin and type IV collagen through its glycosaminoglycan chains.
- 947
- D. KeeneL. SakaiH. BächingerR. Burgeson
- 1987
Biology, Materials Science
The Journal of cell biology
It is suggested that fibrils of skin, tendon, and amnion (and presumably many other tissues that contain both types I and III collagens) are copolymers of at least types I.
- 261 [PDF]
- B. DubletM. E. van der Rest
- 1991
Biology, Materials Science
The Journal of biological chemistry
It is proposed to call the molecule from which this fragment is derived, type XIV collagen, with a chain composition (alpha 1 (XIV]3.3) based on the presence of a domain similar to the COL1 domain of collagens types IX and XII, which suggests thattype XIV collagen belongs to the group of fibril-associated collagen with interrupted triple helices (FACIT).
- 64
- PDF
- Y. MuragakiO. JacenkoS. ApteM. MatteiY. NinomiyaB. Olsen
- 1991
Biology, Medicine
The Journal of biological chemistry
The identification and characterization of a collagen gene encoding a polypeptide which is co-expressed with the alpha 1(VIII) chain in corneal endothelial cells is reported on.
- 78
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