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LILACS e MDL

Sialic Acid Binding Ig-like Lectin 3 .
Antigens, CD33 .
CD33 Antigen .
CD33 Antigens .
Glycoprotein gp67 .
Siglec-3 .
Antigen, CD33 .
Sialic Acid Binding Ig like Lectin 3 .
gp67, Glycoprotein .
A 67-kDa sialic acid binding lectin that is specific for MYELOID CELLS and MONOCYTE-MACROPHAGE PRECURSOR CELLS. This protein is the smallest siglec subtype and contains a single immunoglobulin C2-set domain. It may play a role in intracellular signaling via its interaction with SHP-1 PROTEIN-TYROSINE PHOSPHATASE and SHP-2 PROTEIN-TYROSINE PHOSPHATASE. .
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Sialic Acid Binding Immunoglobulin-like Lectins .
Sialic Acid Binding Ig-like Lectin .
Sialic Acid-binding Hemagglutinin .
Siglec .
Siglecs .
Hemagglutinin, Sialic Acid-binding .
Sialic Acid Binding Ig like Lectin .
Sialic Acid Binding Immunoglobulin like Lectins .
Sialic Acid binding Hemagglutinin .
A family of SIALIC ACID binding proteins found in vertebrate species. They are transmembrane proteins which act as cell surface receptors for a variety of sialylated GLYCOCONJUGATES. While a subset of siglec protein subtypes are evolutionarily conserved between mammalian species, there are many others that are species specific. .
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Sialic Acid Binding Ig-like Lectin 1 .
Antigens, CD169 .
CD169 Antigens .
Sialoadhesin .
Siglec-1 .
Sialic Acid Binding Ig like Lectin 1 .
A sialic acid binding lectin that was originally identified as an adhesion molecule for inflammatory MACROPHAGES and activated MONOCYTES. This protein is the largest known siglec subtype and contains 16 immunoglobulin C2-set domains. It plays a role in cell to cell interactions and interactions with bacteria. .
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Sialic Acid Binding Ig-like Lectin 2 .
CD22 Antigen .
CD22 Glycoprotein .
Siglec-2 .
Antigen, CD22 .
B Lymphocyte Cell Adhesion Molecule .
Glycoprotein, CD22 .
Sialic Acid Binding Ig like Lectin 2 .
Antigens, CD22 .
B-Lymphocyte Cell Adhesion Molecule .
CD22 Antigens .
A lectin and cell adhesion molecule found in B-LYMPHOCYTES. It interacts with SIALIC ACIDS and mediates signaling from B-CELL ANTIGEN RECEPTORS. .
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Myelin-Associated Glycoprotein .
Large Myelin-Associated Glycoprotein Isoform .
Sialic Acid Binding Ig-Like Lectin 4A .
Sialic Acid Binding Ig-like Lectin 4 .
Siglec-4 .
Small Myelin-Associated Glycoprotein Isoform .
Large Myelin Associated Glycoprotein Isoform .
Myelin Associated Glycoprotein .
Sialic Acid Binding Ig Like Lectin 4A .
Sialic Acid Binding Ig like Lectin 4 .
Siglec 4 .
Small Myelin Associated Glycoprotein Isoform .
MAG Protein .
A myelin protein found in the periaxonal membrane of both the central and peripheral nervous systems myelin sheaths. It binds to cells surface receptors found on AXONS and may regulate cellular interactions between MYELIN and AXONS. .
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COP9 Signalosome Complex .
COP9 Signalosome (CSN) .
COP9 Signalosome Subunit 1 .
COP9 Signalosome Subunit 2 .
COP9 Signalosome Subunit 3 .
COP9 Signalosome Subunit 4 .
COP9 Signalosome Subunit 5 .
COP9 Signalosome Subunit 6 .
COP9 Signalosome Subunit 7A .
COP9 Signalosome Subunit 7B .
COP9 Signalosome Subunit 8 .
COP9 Signalsome .
Constitutive Photomorphogenesis 9 Signalosome .
Constitutive Photomorphogenesis 9 Signalsome .
FUSCA Protein 11 .
G Protein Pathway Suppressor 1 .
Sgn3 33137 .
Signalosome Subunit 3 .
Signalosome Complex, COP9 .
Signalsome, COP9 .
Subunit 3, Signalosome .
A multiprotein complex that functions as a peptide hydrolase, or isopeptidase to cleave NEDD8 PROTEIN from the CULLIN and UBIQUITIN-PROTEIN LIGASES, controlling the activity of the ligases. It is highly conserved in eukaryotes and typically consists of 8 subunits (CSN 1-8 proteins). The COP9 signalosome was originally identified in plants, where it controls gene transcription in response to light. .
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RNA 3' Polyadenylation Signals .
3' Polyadenylation Signal .
AAUAAA RNA Sequence .
RNA 3' Polyadenylation Signal .
3' Polyadenylation Signals .
AAUAAA RNA Sequences .
Polyadenylation Signal, 3' .
RNA Sequence, AAUAAA .
Sequence, AAUAAA RNA .
Sequences, AAUAAA RNA .
Signals, 3' Polyadenylation .
Sequences found near the 3' end of MESSENGER RNA that direct the cleavage and addition of multiple ADENINE NUCLEOTIDES to the 3' end of mRNA. .
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