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Domains of laminin

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Domains of laminin. / Engvall, E; Wewer, U M.

I: Journal of Cellular Biochemistry, Bind 61, Nr. 4, 15.06.1996, s. 493-501.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Engvall, E & Wewer, UM 1996, 'Domains of laminin', Journal of Cellular Biochemistry, bind 61, nr. 4, s. 493-501. https://doi.org/10.1002/(SICI)1097-4644(19960616)61:4<493::AID-JCB2>3.0.CO;2-J

APA

Engvall, E., & Wewer, U. M. (1996). Domains of laminin. Journal of Cellular Biochemistry, 61(4), 493-501. https://doi.org/10.1002/(SICI)1097-4644(19960616)61:4<493::AID-JCB2>3.0.CO;2-J

Vancouver

Engvall E, Wewer UM. Domains of laminin. Journal of Cellular Biochemistry. 1996 jun 15;61(4):493-501. https://doi.org/10.1002/(SICI)1097-4644(19960616)61:4<493::AID-JCB2>3.0.CO;2-J

Author

Engvall, E ; Wewer, U M. / Domains of laminin. I: Journal of Cellular Biochemistry. 1996 ; Bind 61, Nr. 4. s. 493-501.

Bibtex

@article{0711e69359194b568150f5820e535b59,
title = "Domains of laminin",
abstract = "Extracellular matrix molecules are often very large and made up of several independent domains, frequently with autonomous activities. Laminin is no exception. A number of globular and rod-like domains can be identified in laminin and its isoforms by sequence analysis as well as by electron microscopy. Here we present the structure-function relations in laminins by examination of their individual domains. This approach to viewing laminin is based on recent results from several laboratories. First, some mutations in laminin genes that cause disease have affected single laminin domains, and some laminin isoforms lack particular domains. These mutants and isoforms are informative with regard to the activities of the mutated and missing domains. These mutants and isoforms are informative with regard to the activities of the mutated and missing domains. Second, laminin-like domains have now been found in a number of other proteins, and data on these proteins may be informative in terms of structure-function relationships in laminin. Finally, a large body of data has accumulated on the structure and activities of proteolytic fragments, recombinant fragments, and synthetic peptides from laminin. The proposed activities of these domains can now be confirmed and extended by in vivo experiments.",
keywords = "Animals, Humans, Laminin, Polymers, Protein Structure, Secondary, Protein Structure, Tertiary, Structure-Activity Relationship",
author = "E Engvall and Wewer, {U M}",
year = "1996",
month = "6",
day = "15",
doi = "10.1002/(SICI)1097-4644(19960616)61:4<493::AID-JCB2>3.0.CO;2-J",
language = "English",
volume = "61",
pages = "493--501",
journal = "Journal of Cellular Biochemistry",
issn = "0730-2312",
publisher = "JohnWiley & Sons, Inc.",
number = "4",

}

RIS

TY - JOUR

T1 - Domains of laminin

AU - Engvall, E

AU - Wewer, U M

PY - 1996/6/15

Y1 - 1996/6/15

N2 - Extracellular matrix molecules are often very large and made up of several independent domains, frequently with autonomous activities. Laminin is no exception. A number of globular and rod-like domains can be identified in laminin and its isoforms by sequence analysis as well as by electron microscopy. Here we present the structure-function relations in laminins by examination of their individual domains. This approach to viewing laminin is based on recent results from several laboratories. First, some mutations in laminin genes that cause disease have affected single laminin domains, and some laminin isoforms lack particular domains. These mutants and isoforms are informative with regard to the activities of the mutated and missing domains. These mutants and isoforms are informative with regard to the activities of the mutated and missing domains. Second, laminin-like domains have now been found in a number of other proteins, and data on these proteins may be informative in terms of structure-function relationships in laminin. Finally, a large body of data has accumulated on the structure and activities of proteolytic fragments, recombinant fragments, and synthetic peptides from laminin. The proposed activities of these domains can now be confirmed and extended by in vivo experiments.

AB - Extracellular matrix molecules are often very large and made up of several independent domains, frequently with autonomous activities. Laminin is no exception. A number of globular and rod-like domains can be identified in laminin and its isoforms by sequence analysis as well as by electron microscopy. Here we present the structure-function relations in laminins by examination of their individual domains. This approach to viewing laminin is based on recent results from several laboratories. First, some mutations in laminin genes that cause disease have affected single laminin domains, and some laminin isoforms lack particular domains. These mutants and isoforms are informative with regard to the activities of the mutated and missing domains. These mutants and isoforms are informative with regard to the activities of the mutated and missing domains. Second, laminin-like domains have now been found in a number of other proteins, and data on these proteins may be informative in terms of structure-function relationships in laminin. Finally, a large body of data has accumulated on the structure and activities of proteolytic fragments, recombinant fragments, and synthetic peptides from laminin. The proposed activities of these domains can now be confirmed and extended by in vivo experiments.

KW - Animals

KW - Humans

KW - Laminin

KW - Polymers

KW - Protein Structure, Secondary

KW - Protein Structure, Tertiary

KW - Structure-Activity Relationship

U2 - 10.1002/(SICI)1097-4644(19960616)61:4<493::AID-JCB2>3.0.CO;2-J

DO - 10.1002/(SICI)1097-4644(19960616)61:4<493::AID-JCB2>3.0.CO;2-J

M3 - Journal article

C2 - 8806072

VL - 61

SP - 493

EP - 501

JO - Journal of Cellular Biochemistry

JF - Journal of Cellular Biochemistry

SN - 0730-2312

IS - 4

ER -

ID: 34326069