The PLAC1-homology region of the ZP domain is sufficient for protein polymerisation.
about
Zona pellucida glycoproteinsStructure of betaglycan zona pellucida (ZP)-C domain provides insights into ZP-mediated protein polymerization and TGF- bindingPlacenta-specific protein 1 is conserved throughout the Placentalia under purifying selectionDEX-1 and DYF-7 establish sensory dendrite length by anchoring dendritic tips during cell migration.A common 'aggregation-prone' interface possibly participates in the self-assembly of human zona pellucida proteins.'ZP domain' of human zona pellucida glycoprotein-1 binds to human spermatozoa and induces acrosomal exocytosis.Structural analysis of peptide-analogues of human Zona Pellucida ZP1 protein with amyloidogenic properties: insights into mammalian Zona Pellucida formationPLAC1 (Placenta-specific 1): a novel, X-linked gene with roles in reproductive and cancer biology.From molecules to mating: Rapid evolution and biochemical studies of reproductive proteins.PLAC1 Expression Decreases in Chorionic Villi in Response to Labor.Phylogenetic analysis and identification of pseudogenes reveal a progressive loss of zona pellucida genes during evolution of vertebrates.The nexus of prematurity, birth defects, and intrauterine growth restriction: a role for plac1-regulated pathways.Evolution, structure, and synthesis of vertebrate egg-coat proteins.Analysis of uromodulin polymerization provides new insights into the mechanisms regulating ZP domain-mediated protein assembly.The Hinge Region of Bovine Zona Pellucida Glycoprotein ZP3 Is Involved in the Formation of the Sperm-Binding Active ZP3/ZP4 Complex.The oncoplacental gene placenta-specific protein 1 is highly expressed in endometrial tumors and cell linesStructural studies of "aggregation-prone" peptide-analogues of teleostean egg chorion ZPB proteins.Tamm-Horsfall Protein Regulates Mononuclear Phagocytes in the Kidney.Immunohistochemical characterization of novel murine monoclonal antibodies against human placenta-specific 1.The "ZP domain" is not one, but likely two independent domains.
P2860
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P2860
The PLAC1-homology region of the ZP domain is sufficient for protein polymerisation.
description
2006 nî lūn-bûn
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2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2006年の論文
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2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
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name
The PLAC1-homology region of the ZP domain is sufficient for protein polymerisation.
@ast
The PLAC1-homology region of the ZP domain is sufficient for protein polymerisation.
@en
type
label
The PLAC1-homology region of the ZP domain is sufficient for protein polymerisation.
@ast
The PLAC1-homology region of the ZP domain is sufficient for protein polymerisation.
@en
prefLabel
The PLAC1-homology region of the ZP domain is sufficient for protein polymerisation.
@ast
The PLAC1-homology region of the ZP domain is sufficient for protein polymerisation.
@en
P2093
P2860
P356
P1433
P1476
The PLAC1-homology region of the ZP domain is sufficient for protein polymerisation.
@en
P2093
Eveline S Litscher
Paul M Wassarman
William G Janssen
P2860
P2888
P356
10.1186/1471-2091-7-11
P50
P577
2006-04-06T00:00:00Z
P5875
P6179
1043044640