author_facet Xiong, Jian-Ping
Stehle, Thilo
Goodman, Simon L.
Arnaout, M. Amin
Xiong, Jian-Ping
Stehle, Thilo
Goodman, Simon L.
Arnaout, M. Amin
author Xiong, Jian-Ping
Stehle, Thilo
Goodman, Simon L.
Arnaout, M. Amin
spellingShingle Xiong, Jian-Ping
Stehle, Thilo
Goodman, Simon L.
Arnaout, M. Amin
Blood
New insights into the structural basis of integrin activation
Cell Biology
Hematology
Immunology
Biochemistry
author_sort xiong, jian-ping
spelling Xiong, Jian-Ping Stehle, Thilo Goodman, Simon L. Arnaout, M. Amin 0006-4971 1528-0020 American Society of Hematology Cell Biology Hematology Immunology Biochemistry http://dx.doi.org/10.1182/blood-2003-01-0334 <jats:title>Abstract</jats:title><jats:p>Integrins are cell adhesion receptors that communicate biochemical and mechanical signals in a bidirectional manner across the plasma membrane and thus influence most cellular functions. Intracellular signals switch integrins into a ligand-competent state as a result of elicited conformational changes in the integrin ectodomain. Binding of extracellular ligands induces, in turn, structural changes that convey distinct signals to the cell interior. The structural basis of this bidirectional signaling has been the focus of intensive study for the past 3 decades. In this perspective, we develop a new hypothesis for integrin activation based on recent crystallographic, electron microscopic, and biochemical studies.</jats:p> New insights into the structural basis of integrin activation Blood
doi_str_mv 10.1182/blood-2003-01-0334
facet_avail Online
Free
finc_class_facet Biologie
Medizin
Chemie und Pharmazie
format ElectronicArticle
fullrecord blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTE4Mi9ibG9vZC0yMDAzLTAxLTAzMzQ
id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTE4Mi9ibG9vZC0yMDAzLTAxLTAzMzQ
institution DE-Zwi2
DE-D161
DE-Gla1
DE-Zi4
DE-15
DE-Pl11
DE-Rs1
DE-105
DE-14
DE-Ch1
DE-L229
DE-D275
DE-Bn3
DE-Brt1
imprint American Society of Hematology, 2003
imprint_str_mv American Society of Hematology, 2003
issn 0006-4971
1528-0020
issn_str_mv 0006-4971
1528-0020
language English
mega_collection American Society of Hematology (CrossRef)
match_str xiong2003newinsightsintothestructuralbasisofintegrinactivation
publishDateSort 2003
publisher American Society of Hematology
recordtype ai
record_format ai
series Blood
source_id 49
title New insights into the structural basis of integrin activation
title_unstemmed New insights into the structural basis of integrin activation
title_full New insights into the structural basis of integrin activation
title_fullStr New insights into the structural basis of integrin activation
title_full_unstemmed New insights into the structural basis of integrin activation
title_short New insights into the structural basis of integrin activation
title_sort new insights into the structural basis of integrin activation
topic Cell Biology
Hematology
Immunology
Biochemistry
url http://dx.doi.org/10.1182/blood-2003-01-0334
publishDate 2003
physical 1155-1159
description <jats:title>Abstract</jats:title><jats:p>Integrins are cell adhesion receptors that communicate biochemical and mechanical signals in a bidirectional manner across the plasma membrane and thus influence most cellular functions. Intracellular signals switch integrins into a ligand-competent state as a result of elicited conformational changes in the integrin ectodomain. Binding of extracellular ligands induces, in turn, structural changes that convey distinct signals to the cell interior. The structural basis of this bidirectional signaling has been the focus of intensive study for the past 3 decades. In this perspective, we develop a new hypothesis for integrin activation based on recent crystallographic, electron microscopic, and biochemical studies.</jats:p>
container_issue 4
container_start_page 1155
container_title Blood
container_volume 102
format_de105 Article, E-Article
format_de14 Article, E-Article
format_de15 Article, E-Article
format_de520 Article, E-Article
format_de540 Article, E-Article
format_dech1 Article, E-Article
format_ded117 Article, E-Article
format_degla1 E-Article
format_del152 Buch
format_del189 Article, E-Article
format_dezi4 Article
format_dezwi2 Article, E-Article
format_finc Article, E-Article
format_nrw Article, E-Article
_version_ 1792348160078643203
geogr_code not assigned
last_indexed 2024-03-01T18:06:45.811Z
geogr_code_person not assigned
openURL url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=New+insights+into+the+structural+basis+of+integrin+activation&rft.date=2003-08-15&genre=article&issn=1528-0020&volume=102&issue=4&spage=1155&epage=1159&pages=1155-1159&jtitle=Blood&atitle=New+insights+into+the+structural+basis+of+integrin+activation&aulast=Arnaout&aufirst=M.+Amin&rft_id=info%3Adoi%2F10.1182%2Fblood-2003-01-0334&rft.language%5B0%5D=eng
SOLR
_version_ 1792348160078643203
author Xiong, Jian-Ping, Stehle, Thilo, Goodman, Simon L., Arnaout, M. Amin
author_facet Xiong, Jian-Ping, Stehle, Thilo, Goodman, Simon L., Arnaout, M. Amin, Xiong, Jian-Ping, Stehle, Thilo, Goodman, Simon L., Arnaout, M. Amin
author_sort xiong, jian-ping
container_issue 4
container_start_page 1155
container_title Blood
container_volume 102
description <jats:title>Abstract</jats:title><jats:p>Integrins are cell adhesion receptors that communicate biochemical and mechanical signals in a bidirectional manner across the plasma membrane and thus influence most cellular functions. Intracellular signals switch integrins into a ligand-competent state as a result of elicited conformational changes in the integrin ectodomain. Binding of extracellular ligands induces, in turn, structural changes that convey distinct signals to the cell interior. The structural basis of this bidirectional signaling has been the focus of intensive study for the past 3 decades. In this perspective, we develop a new hypothesis for integrin activation based on recent crystallographic, electron microscopic, and biochemical studies.</jats:p>
doi_str_mv 10.1182/blood-2003-01-0334
facet_avail Online, Free
finc_class_facet Biologie, Medizin, Chemie und Pharmazie
format ElectronicArticle
format_de105 Article, E-Article
format_de14 Article, E-Article
format_de15 Article, E-Article
format_de520 Article, E-Article
format_de540 Article, E-Article
format_dech1 Article, E-Article
format_ded117 Article, E-Article
format_degla1 E-Article
format_del152 Buch
format_del189 Article, E-Article
format_dezi4 Article
format_dezwi2 Article, E-Article
format_finc Article, E-Article
format_nrw Article, E-Article
geogr_code not assigned
geogr_code_person not assigned
id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTE4Mi9ibG9vZC0yMDAzLTAxLTAzMzQ
imprint American Society of Hematology, 2003
imprint_str_mv American Society of Hematology, 2003
institution DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1
issn 0006-4971, 1528-0020
issn_str_mv 0006-4971, 1528-0020
language English
last_indexed 2024-03-01T18:06:45.811Z
match_str xiong2003newinsightsintothestructuralbasisofintegrinactivation
mega_collection American Society of Hematology (CrossRef)
physical 1155-1159
publishDate 2003
publishDateSort 2003
publisher American Society of Hematology
record_format ai
recordtype ai
series Blood
source_id 49
spelling Xiong, Jian-Ping Stehle, Thilo Goodman, Simon L. Arnaout, M. Amin 0006-4971 1528-0020 American Society of Hematology Cell Biology Hematology Immunology Biochemistry http://dx.doi.org/10.1182/blood-2003-01-0334 <jats:title>Abstract</jats:title><jats:p>Integrins are cell adhesion receptors that communicate biochemical and mechanical signals in a bidirectional manner across the plasma membrane and thus influence most cellular functions. Intracellular signals switch integrins into a ligand-competent state as a result of elicited conformational changes in the integrin ectodomain. Binding of extracellular ligands induces, in turn, structural changes that convey distinct signals to the cell interior. The structural basis of this bidirectional signaling has been the focus of intensive study for the past 3 decades. In this perspective, we develop a new hypothesis for integrin activation based on recent crystallographic, electron microscopic, and biochemical studies.</jats:p> New insights into the structural basis of integrin activation Blood
spellingShingle Xiong, Jian-Ping, Stehle, Thilo, Goodman, Simon L., Arnaout, M. Amin, Blood, New insights into the structural basis of integrin activation, Cell Biology, Hematology, Immunology, Biochemistry
title New insights into the structural basis of integrin activation
title_full New insights into the structural basis of integrin activation
title_fullStr New insights into the structural basis of integrin activation
title_full_unstemmed New insights into the structural basis of integrin activation
title_short New insights into the structural basis of integrin activation
title_sort new insights into the structural basis of integrin activation
title_unstemmed New insights into the structural basis of integrin activation
topic Cell Biology, Hematology, Immunology, Biochemistry
url http://dx.doi.org/10.1182/blood-2003-01-0334