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Results: 221 to 229 of 229

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A new family of yeast nuclear pore complex proteins.
Wente SR, Rout MP, Blobel G
(1992) J Cell Biol 119: 705-23
MeSH Terms: Amino Acid Sequence, Antibodies, Monoclonal, Base Sequence, DNA Transposable Elements, DNA, Fungal, Epitopes, Fungal Proteins, Genes, Fungal, Membrane Proteins, Microscopy, Fluorescence, Microscopy, Immunoelectron, Molecular Sequence Data, Nuclear Envelope, Nuclear Pore Complex Proteins, Nuclear Proteins, Protein Structure, Secondary, RNA, Transfer, His, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Show Abstract · Added March 21, 2014
We have identified a novel family of yeast nuclear pore complex proteins. Three individual members of this family, NUP49, NUP100, and NUP116, have been isolated and then characterized by a combination of molecular genetics and immunolocalization. Employing immunoelectron and immunofluorescence microscopy on yeast cells, we found that the binding of a polyspecific monoclonal antibody recognizing this family was predominantly at the nuclear pore complexes. Furthermore, the tagging of NUP49 with a unique epitope enabled the immunolocalization of this protein to the nuclear pore complex by both fluorescence and electron microscopy. DNA sequence analysis has shown that the amino-terminal regions of NUP49, NUP100, and NUP116 share repeated "GLFG" motifs separated from each other by glutamine, asparagine, serine and threonine rich spacers. All three proteins lack a repetitive domain found in the two precisely described yeast nuclear pore complex proteins. Only NUP49 is essential for cell viability. NUP116-deficient cells grow very slowly and are temperature sensitive, whereas the lack of NUP100 has no detectable phenotype. NUP100 and NUP116 are homologous over their entire lengths. Interestingly, NUP100 and NUP116 are both flanked by a histidine tRNA gene and a transposon element suggesting that they may have arisen by gene duplication. We propose that subfamilies of pore complex proteins can be defined by their characteristic combinations of different modular domains.
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19 MeSH Terms
NH2-terminal modification of the phosphatase 2A catalytic subunit allows functional expression in mammalian cells.
Wadzinski BE, Eisfelder BJ, Peruski LF, Mumby MC, Johnson GL
(1992) J Biol Chem 267: 16883-8
MeSH Terms: Amino Acid Sequence, Animals, Antibodies, Monoclonal, Base Sequence, Cell Line, DNA, Viral, Epitopes, Hemagglutinin Glycoproteins, Influenza Virus, Hemagglutinins, Viral, Kinetics, Macromolecular Substances, Molecular Sequence Data, Oligodeoxyribonucleotides, Phosphoprotein Phosphatases, Polymerase Chain Reaction, Protein Phosphatase 2, Recombinant Proteins, Restriction Mapping, Viral Envelope Proteins
Show Abstract · Added December 10, 2013
Functional expression of recombinant wild-type phosphatase 2A catalytic subunit has been unsuccessful in the past. A nine-amino-acid peptide sequence (YP-YDVPDYA) derived from the influenza hemagglutinin protein was used to modify the NH2 and/or COOH terminus of the phosphatase 2A catalytic subunit. Addition of the nine-amino-acid sequence at the NH2 terminus allowed recombinant phosphatase 2A expression as a predominantly cytosolic phosphatase 2A enzyme. The 12CA5 monoclonal antibody that recognizes the nine-amino-acid hemagglutinin peptide sequence was used to immunoprecipitate the epitope-tagged phosphatase 2A catalytic subunit. Assay of the immunoprecipitated epitope-tagged phosphatase 2A demonstrated an okadaic acid-sensitive dephosphorylation of [32P] histone H1 and [32P]myelin basic protein similar to that measured with the wild-type enzyme. Functional phosphatase activity could be demonstrated for the NH2-terminal modified phosphatase 2A catalytic subunit following transient expression in COS cells or stable expression in Rat1a cells. In contrast, the COOH-terminal-modified phosphatase 2A catalytic subunit was very poorly expressed. The NH2-, COOH-modified subunit, having the nine-amino-acid hemagglutinin peptide sequence encoded at both termini of the polypeptide, was also expressed as a functional phosphatase 2A enzyme. Thus, NH2-terminal modification of the phosphatase 2A catalytic subunit results in a functional plasmid-expressed enzyme. The unique nine-amino-acid epitope-tag sequence also provides a method to easily resolve the recombinant phosphatase 2A from the endogenous wild-type gene product and related phosphatases expressed in cells.
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19 MeSH Terms
Mapping the orientation of an antigenic peptide bound in the antigen binding groove of H-2Kb using a monoclonal antibody.
Joyce S, Sun R, Nathenson SG
(1992) Biochem Biophys Res Commun 186: 1449-54
MeSH Terms: Abelson murine leukemia virus, Amino Acid Sequence, Animals, Antibodies, Monoclonal, B-Lymphocytes, Cell Line, Epitopes, Genes, MHC Class I, H-2 Antigens, Mice, Models, Molecular, Molecular Sequence Data, Polymerase Chain Reaction, Protein Conformation, Rauscher Virus, T-Lymphocytes
Show Abstract · Added October 2, 2015
The major histocompatibility complex class I molecules are receptors for intracellular peptides, both of self and non-self origin. When non-self peptides (eg., pathogen derived) are bound to the class I molecules, they form ligands for T cell receptors resulting in antigen specific lysis of the infected cells by cytotoxic T lymphocytes. Therefore, an understanding of the process of antigen recognition requires the precise definition of the structural features of the bimolecular complex formed by a single well defined antigenic peptide bound to the class I molecule. A strategy using antibodies was developed to probe the structural features of the H-2Kb containing a defined peptide in the antigen cleft. We report that the binding surface area of a Kb specific monoclonal antibody (28-13-3s) includes residues in the alpha 1 (Gly56 and Glu58) and alpha 2 (Trp167) helices of Kb thus, binding across the antigen binding groove. When cells treated with the antigenic peptide of vesicular stomatitis virus, N52-59, and its alanine substituted analogs were tested for 28-13-3s binding, it was found that position 1 of the peptide also forms a part of the antibody binding site. This finding strongly supports the positioning of the N-terminus of N52-59 proximal to pocket A, thus, assuming an orientation parallel to the alpha 1 helix.
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16 MeSH Terms
Immunolocalization of integrin alpha 6 beta 4 in mouse junctional epithelium suggests an anchoring function to both the internal and the external basal lamina.
Hormia M, Virtanen I, Quaranta V
(1992) J Dent Res 71: 1503-8
MeSH Terms: Animals, Antigens, Surface, Basement Membrane, Cell Adhesion, Cell Membrane, Collagen, Epithelium, Epitopes, Fluorescent Antibody Technique, Gingiva, Integrin alpha6beta4, Integrins, Keratinocytes, Laminin, Mice, Mice, Inbred C57BL, Mice, Inbred Strains
Show Abstract · Added March 27, 2014
The localization of the integrin alpha 6 beta 4, a transmembrane adhesion molecule associated with hemidesmosomes, was studied in mouse junctional epithelium (JE) by the use of monoclonal antibodies in indirect immunofluorescence microscopy. The results showed that the integrin a6 subunit was expressed throughout the JE and was localized to the cell membranes, including the aspects facing the internal and external basal laminae. The beta 4 subunit had a more restricted distribution. It was expressed only in cells facing the internal and the external basal laminae and had a basally polarized distribution. In other parts of gingival epithelium, both integrin subunits were mainly expressed at the basal aspects of basal epithelial cells. The basement membrane components, type IV collagen and laminin, could be detected only in the external basal lamina and in other basement membranes of gingival epithelium. The results indicate that the a6 beta 4 integrin, expressed in mouse JE, has a role in mediating the attachment of the cells to the basement membranes facing the connective tissue and the tooth.
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17 MeSH Terms
A polymorphic human kidney-specific non-MHC alloantigen. Its possible role in tissue-specific allograft immunity.
Joyce S, Mathew JM, Flye MW, Mohanakumar T
(1992) Transplantation 53: 1119-27
MeSH Terms: Animals, Blotting, Western, Epitopes, Graft Rejection, Haplorhini, Histocompatibility Antigens, Humans, Immune Sera, Immunity, Immunohistochemistry, Isoantigens, Kidney, Kidney Transplantation, Peptide Mapping, Polymorphism, Genetic, Transplantation, Homologous
Show Abstract · Added October 2, 2015
Tissue specific non-MHC alloantigens play a crucial role in allograft immunity. However, their structural properties have remained elusive, largely due to their inability to induce a strong antibody response. We report the characterization of a monkey heteroantiserum, MHK-I, raised against human kidney cells, that serologically reacts specifically with kidney cells after extensive absorptions of anti-HLA class I and II reactivities. The non-MHC MHK-I-binding molecule(s) is expressed only in the renal cortex on the glomerulus, peritubular capillaries, venous endothelium, and tubular epithelium. Immunochemically, MHK-I recognizes a kidney-specific non-MHC alloantigen of Mr 90,000 to 100,000 (90 kD). These properties of MHK-I are similar to those of the previously characterized alloantibodies eluted from rejected kidneys. These alloantibodies bind to the kidney from which the antibody was eluted and to a few others but are unlike MHK-I, which binds to extracts prepared from all human kidneys. Biochemical analysis by two-dimensional electrophoresis (pI ranging between 4.5 and 5.5) and peptide fingerprinting provide further evidence that the alloantigen is polymorphic. These findings imply that the non-MHC kidney-specific molecule(s) may function as target(s) for immune destruction of renal allografts.
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16 MeSH Terms
Binding of type 3 reovirus by a domain of the sigma 1 protein important for hemagglutination leads to infection of murine erythroleukemia cells.
Rubin DH, Wetzel JD, Williams WV, Cohen JA, Dworkin C, Dermody TS
(1992) J Clin Invest 90: 2536-42
MeSH Terms: Animals, Antibodies, Monoclonal, Antigens, Viral, Capsid Proteins, Epitopes, Hemagglutination, In Vitro Techniques, L Cells, Leukemia, Erythroblastic, Acute, Mammalian orthoreovirus 3, Mice, Receptors, Virus, Tumor Cells, Cultured, Viral Proteins, Virus Replication
Show Abstract · Added December 10, 2013
The recognition of cellular receptors by the mammalian reoviruses is an important determinant of cell and tissue tropism exhibited by reovirus strains of different serotypes. To extend our knowledge of the role of reovirus-receptor interactions in reovirus tropism, we determined whether type 1 and type 3 reovirus strains can infect cells derived from erythrocyte precursors. We found that reovirus type 3 Dearing (T3D), but not type 1 Lang, can grow in murine erythroleukemia (MEL) cells. This difference in growth was investigated by using reassortant viruses and we found that the capacity of T3D to infect MEL cells is determined by the viral cell-attachment protein, sigma 1. In experiments using murine monoclonal antibodies (mAbs) that bind to different sigma 1 regions, we show that T3D binding to MEL cells is inhibited by a mAb that identifies a domain important for hemagglutination (HA). We also determined that type 3 strains that can infect murine L cells but do not produce HA do not infect MEL cells. These results suggest that type 3 reovirus binds to and infects erythrocyte precursor cells via a sigma 1 domain important for HA. Moreover, this study suggests that different domains of some viral cell-attachment proteins are used to initiate productive infections of different types of cells.
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15 MeSH Terms
Characterization of the specificity of DR monoclonal antibodies.
Molinaro GA, Quaranta V, Ferrone S
(1979) Transplant Proc 11: 1748-50
MeSH Terms: Animals, Antibody Specificity, B-Lymphocytes, Clone Cells, Cytotoxicity, Immunologic, Epitopes, HLA Antigens, Humans, Immune Sera, Immunoglobulin Fab Fragments, Mice, Mice, Inbred BALB C, Mice, Inbred NZB
Added March 27, 2014
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13 MeSH Terms
Lack of DR antigens on human B-lymphocyte-mouse fibroblast hybrids that express HLA-A,B antigens.
Glassy MC, Pellegrino MA, Quaranta V, Molinaro GA, Ferrone S
(1979) Transplant Proc 11: 1719-21
MeSH Terms: Animals, B-Lymphocytes, Cell Differentiation, Cell Line, Chromosomes, Human, 6-12 and X, Clone Cells, Epitopes, Fibroblasts, HLA Antigens, Humans, Hybrid Cells, Mice, Polymorphism, Genetic, Rabbits
Added March 27, 2014
1 Communities
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14 MeSH Terms
Site-specific anti-cytochrome c antibodies. Inhibition of the reactions between cytochrome c and its respiratory chain electron exchange partners.
Osheroff N, Jemmerson R, Speck SH, Ferguson-Miller S, Margoliash E
(1979) J Biol Chem 254: 12717-24
MeSH Terms: Animals, Antibodies, Antigen-Antibody Complex, Binding Sites, Antibody, Cytochrome c Group, Electron Transport, Epitopes, Horses, Immunoglobulin Fab Fragments, Kinetics, Models, Molecular, Protein Conformation, Rabbits
Added March 5, 2014
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13 MeSH Terms