1
40
2
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1042/bj2480837" target="_blank" rel="noreferrer noopener">http://doi.org/10.1042/bj2480837</a>
Rights
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
Pages
837-845
Issue
3
Volume
248
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Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
Mouse Alpha-macroglobulin - Structure, Function And A Molecular-model
Publisher
An entity responsible for making the resource available
Biochemical Journal
Date
A point or period of time associated with an event in the lifecycle of the resource
1987
1987-12
Subject
The topic of the resource
Biochemistry & Molecular Biology; Cell Biology; Life Sciences & Biomedicine - Other; Topics
Creator
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Hudson N W; Kehoe J M; Koo P H
Identifier
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<a href="http://doi.org/10.1042/bj2480837" target="_blank" rel="noreferrer noopener">10.1042/bj2480837</a>
Format
The file format, physical medium, or dimensions of the resource
Journal Article or Conference Abstract Publication
1987
Biochemical Journal
Biochemistry & Molecular Biology
Cell Biology
Hudson N W
Journal Article or Conference Abstract Publication
Kehoe J M
Koo P H
Life Sciences & Biomedicine - Other
Topics
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1042/0264-6021:3510503" target="_blank" rel="noreferrer noopener">http://doi.org/10.1042/0264-6021:3510503</a>
Rights
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
Pages
503-508
Volume
351
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Locate full-text within NEOMED Library's e-journal collections
<p>Users with a NEOMED Library login can search for full-text journal articles at the following url: <a href="https://libraryguides.neomed.edu/home">https://libraryguides.neomed.edu/home</a></p>
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
alpha(2)-Macroglobulin modulates the immunoregulatory function of the lipocalin placental protein 14
Publisher
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Biochemical Journal
Date
A point or period of time associated with an event in the lifecycle of the resource
2000
2000-10
Subject
The topic of the resource
alpha-2-macroglobulin; alpha-macroglobulin; binding; Biochemistry & Molecular Biology; factor-beta; glycodelin; human; immunosuppressive; inhibition; nerve growth-factor; phosphorylation; phytohemagglutinin; pregnancy proteins; proteins; receptor; serum carrier; serum transport; signal-transduction
Creator
An entity primarily responsible for making the resource
Riely G J; Rachmilewitz J; Koo P H; Tykocinski M L
Description
An account of the resource
Human placental protein 14 (PP14; also known as glycodelin and progesterone-associatcd endometrial protein) is an immuno-suppressive protein of the lipocalin structural superfamily. Mechanisms regulating serum PP14's inmunosuppressive activity remain to be elucidated. In the present study, an interaction between PP14 and a major serum protein carrier, alpha (2)-macroglobulin (alpha M-2), was documented for the first time. Using native gel electrophoresis, we showed that PP14, as well as its alternative splice variant PP14.2, binds to both alpha M-2 and methylamine-activated (MA)-alpha M-2. Cross-competition studies demonstrated that the variants compete for binding to alpha M-2. PP14 bound to alpha M-2 and MA-alpha M-2 with K-d values of 167+/-70 and 221+/-56 nM (means+/-S.D.) respectively, as determined by surface plasmon resonance. Significantly, the addition of alpha M-2 or MA-alpha M-2 to a T-cell proliferation assay strongly potentiated the inhibitory capacity of PP14. On the basis of these findings, alpha M-2 emerges as the first serum protein that can physically associate with, and thereby regulate, PP14. Moreover, this represents the first documented interaction between the protein carrier alpha M-2 and a lipocalin protein.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1042/0264-6021:3510503" target="_blank" rel="noreferrer noopener">10.1042/0264-6021:3510503</a>
Format
The file format, physical medium, or dimensions of the resource
Journal Article
2000
alpha-2-macroglobulin
alpha-macroglobulin
Binding
Biochemical Journal
Biochemistry & Molecular Biology
factor-beta
Glycodelin
Human
immunosuppressive
inhibition
Journal Article
Koo P H
nerve growth-factor
Phosphorylation
phytohemagglutinin
pregnancy proteins
Proteins
Rachmilewitz J
Receptor
Riely G J
serum carrier
serum transport
signal-transduction
Tykocinski M L