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Results: 201 to 210 of 230

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HLA-DR antigens and mitogenic factors released by PWM-stimulated T lymphocytes share the framework determinant recognized by the monoclonal antibody Q5/13.
Indiveri F, Russo C, Quaranta V, Pellegrino MA, Ferrone S
(1981) Cell Immunol 62: 406-11
MeSH Terms: Adsorption, Antibodies, Monoclonal, B-Lymphocytes, Epitopes, Histocompatibility Antigens Class II, Humans, Interleukin-2, Lymphokines, Pokeweed Mitogens, T-Lymphocytes
Added March 27, 2014
1 Communities
1 Members
0 Resources
10 MeSH Terms
Cross-reactivity between human and murine lymphocyte antigens. IV. Reactivity of H-2 alloantisera with HLA-A, B antigens.
Quaranta V, Pellegrino MA, Callahan GN, Ferrone S
(1981) Immunogenetics 13: 311-7
MeSH Terms: Animals, Cross Reactions, Epitopes, Guinea Pigs, H-2 Antigens, HLA Antigens, Humans, Isoantibodies, Mice, Rabbits, Rats, Species Specificity
Show Abstract · Added March 27, 2014
The anti-H-2 alloantiserum D-32 [(B10.A(2R) x C3H.SW) anti-C3H] is cytolytic to human lymphocytes. Fab2 blocking assays, indirect immunoprecipitation and sequential immunoprecipitation experiments showed that the anti-H-2 alloantiserum D-32 recognizes antigenic determinants which are expressed on the heavy chain of subpopulations of HLA-A, B antigens. These determinants are different from those defining the serological polymorphism of the HLA-A, B, C system, are the same as or spatially close to those recognized by the anti-HLA-A, B monoclonal antibody Q6/64 and are expressed on rabbit, rat or guinea pig lymphocytes.
1 Communities
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12 MeSH Terms
The free and the beta 2-microglobulin-associated heavy chains of HLA-A, B alloantigens share the antigenic determinant recognized by the monoclonal antibody Q1/28.
Quaranta V, Walker LE, Ruberto G, Pellegrino MA, Ferrone S
(1981) Immunogenetics 13: 285-95
MeSH Terms: Antibodies, Monoclonal, B-Lymphocytes, Cell Line, Electrophoresis, Polyacrylamide Gel, Epitopes, HLA Antigens, Humans, Immunosorbent Techniques, beta 2-Microglobulin
Show Abstract · Added March 27, 2014
Serological and immunochemical assays have shown that the monoclonal antibody Q1/28 recognizes an antigenic determinant which is expressed on the heavy chain of subsets of HLA-A, B antigens and is distinct from those defining the serological polymorphism of this system. Association of the HLA-A, B heavy chain with beta 2-microglobulin is not required for expression of the antigenic determinant recognized by the monoclonal antibody Q1/28, since this antibody can immunoprecipitate a 45 000 m.w. component from radiolabeled lymphoid-cell glycoproteins immunodepleted with either an anti-human beta 2-microglobulin xenoantiserum or the MoAb W6/32 to framework determinants of HLA-A, B, C antigens. Furthermore, the MoAb Q1/28 can immunoprecipitate a 45 000 m.w. component from an NP40 lysate of radiolabeled Daudi cells, which lack the genetic information for beta 2-microglobulin. The determinant recognized by the MoAb Q1/28 is relatively resistant to denaturing treatments and does not appear to be carbohydrate in nature. The MoAb Q1/28 is the first example of an antibody which recognizes an antigenic determinant expressed on both the beta 2-microglobulin-associated and free HLA-A, B heavy chains.
1 Communities
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9 MeSH Terms
Distribution of antigenic determinants recognized by three monoclonal antibodies (Q2/70, Q5/6 and Q5/13) on human Ia-like alloantigens and on their subunits.
Quaranta V, Tanigaki N, Ferrone S
(1981) Immunogenetics 12: 175-82
MeSH Terms: Animals, Antibodies, Antigen-Antibody Complex, Binding Sites, Antibody, Chromosome Mapping, Clone Cells, Epitopes, Genetic Code, Goats, Histocompatibility Antigens Class II, Humans, Immune Sera, Mice, Rabbits
Show Abstract · Added March 27, 2014
The distribution of antigenic determinants recognized by the anti-Ia-like antigen monoclonal antibodies (MoAb) Q2/70, Q5/6 and Q5/13 on molecules coded for by the DR locus and by non-DR loci was investigated using a binding assay with 125I-labeled Ia-like antigens isolated from four B lymphoid cell lines. The determinants reacting with the MoAb Q2/70 and Q5/13 are expressed on all DR alloantigens tested and on BR4X7 specificities, while those reacting with the MoAb Q5/6 are not detectable on DRw7 and BR4X7 molecules. None of the monoclonal antibodies reacted with DC1 molecules. The MoAb Q5/6 and Q5/13 reacted with the isolated beta subunit of the Ia-like antigenic complex, while the MoAb Q2/70 did not react with the isolated chains.
1 Communities
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14 MeSH Terms
Isolation of Ia-like antigen-bearing cells from human peripheral lymphocytes through the use of a monoclonal antibody to framework determinants of Ia-like antigens.
Indiveri F, Ng AK, Russo C, Quaranta V, Pellegrino MA, Ferrone S
(1980) J Immunol Methods 39: 343-54
MeSH Terms: Animals, Antibodies, Antibody-Dependent Cell Cytotoxicity, B-Lymphocytes, Cell Separation, Clone Cells, Complement System Proteins, Cytotoxicity, Immunologic, Epitopes, Goats, HLA Antigens, Histocompatibility Antigens Class II, Humans, Lymphocyte Culture Test, Mixed, Lymphocytes, Mice, Rabbits, Rosette Formation, Sheep, T-Lymphocytes
Added March 27, 2014
1 Communities
1 Members
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20 MeSH Terms
Serologic and immunochemical characterization of the specificity of four monoclonal antibodies to distinct antigenic determinants expressed on subpopulations of human Ia-like antigens.
Quaranta V, Pellegrino MA, Ferrone S
(1981) J Immunol 126: 548-52
MeSH Terms: Antibodies, Antibody Specificity, Binding Sites, Antibody, Binding, Competitive, Cell Line, Clone Cells, Epitopes, Histocompatibility Antigens Class II, Humans, Hybrid Cells
Show Abstract · Added March 27, 2014
Serologic and immunochemical assays showed that the monoclonal antibodies Q2/70, Q2/80, Q5/6, and Q5/13 react with human Ia-like antigens. Each monoclonal antibody recognizes distinct antigenic determinants that are different from those defining the serologic polymorphism of Ia-like antigens defined by conventional alloantisera and are expressed on subpopulations of Ia-like antigens. The determinants recognized by the MoAb Q2/70 and Q5/13 are expressed on all HLA-DR allospecificities tested, whereas those reacting with the MoAb Q2/80 and Q5/6 are not detectable on HLA-DR5 and HLA-DR7 allospecificities, respectively.
1 Communities
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10 MeSH Terms
Monoclonal antibodies to HLA-A,B, and Ia-like antigens inhibit colony formation by human myeloid progenitor cells.
Fitchen JH, Ferrone S, Quaranta V, Molinaro GA, Cline MJ
(1980) J Immunol 125: 2004-8
MeSH Terms: Animals, Antilymphocyte Serum, Clone Cells, Colony-Forming Units Assay, Complement System Proteins, Epitopes, HLA Antigens, Hematopoietic Stem Cells, Histocompatibility Antigens Class II, Humans, Isoantibodies, Mice, Rabbits
Show Abstract · Added March 27, 2014
Hybridomas derived from the fusion of murine myeloma cells with splenocytes from mice immunized with human cultured lymphoid cells secreted monoclonal antibodies to human cell surface antigens. Serologic and immunochemical assays showed that 4 monoclonal antibodies (Ab Q2/47, Q2/61, Q2/70, Q2/80) recognize framework determinants of Ia-like antigens and 1 monoclonal antibody (Ab Q1/28) reacts with determinants expressed on the heavy chain of HLA-A,B antigens. Both anti-HLA-A,B and anti-Ia-like antigen monoclonal antibodies caused complement-dependent inhibition of granulocyte-macrophage colony formation by human bone marrow grown in soft agar. Mixing experiments excluded the possibility of an indirect effect on progenitor cells by lysis of auxiliary cells. These results indicate that human myeloid progenitor cells express HLA-A,B and Ia-like antigens.
1 Communities
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13 MeSH Terms
Purification of immunologically functional subsets of human Ia-like antigens on a monoclonal antibody (Q5/13) immunoadsorbent.
Quaranta V, Walker LE, Pellegrino MA, Ferrone S
(1980) J Immunol 125: 1421-5
MeSH Terms: Antibodies, Antigen-Antibody Complex, B-Lymphocytes, Clone Cells, Cytotoxicity, Immunologic, Epitopes, Histocompatibility Antigens Class II, Humans, Immunosorbents, Molecular Weight
Show Abstract · Added March 27, 2014
Serologic and immunochemical asays have shown that the monoclonal antibody Q5/13 recognizes an antigenic determinant expressed on a subset of human Ia-like antigens. Testing with a panel of HLA typed B lymphoid cells has shown that this determinant is different from those defining the serologic polymorphism of HLA-DR antigens. The monoclonal antibody Q5/13 has been used to purify subsets of human Ia-like antigens, which are immunologically functional. These reagents should facilitate the characterization of structural and functional properties of human Ia-like antigens.
1 Communities
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10 MeSH Terms
Inhibition of platelet aggregation by a monoclonal antibody against human fibronectin.
Dixit VM, Haverstick DM, O'Rourke K, Hennessy SW, Broekelmann TJ, McDonald JA, Grant GA, Santoro SA, Frazier WA
(1985) Proc Natl Acad Sci U S A 82: 3844-8
MeSH Terms: Animals, Antibodies, Monoclonal, Calcimycin, Cell Adhesion, Cricetinae, Cricetulus, Dose-Response Relationship, Drug, Electrophoresis, Polyacrylamide Gel, Epitopes, Female, Fibronectins, Humans, Peptide Hydrolases, Platelet Aggregation, Thrombin
Show Abstract · Added March 5, 2014
A monoclonal antibody (A3.3) has been generated against human platelet fibronectin (FN). A3.3 reacts with human plasma FN but with no other plasma proteins. A3.3 was found to inhibit thrombin- or ionophore A23187-stimulated aggregation of gel-filtered platelets in a concentration-dependent manner in both an aggregometer assay and a sensitive well plate aggregation assay. The antibody does not block secretion of serotonin. Four other anti-FN monoclonal antibodies that recognize different epitopes on FN than A3.3 does have no effect on platelet aggregation. A3.3 does not block the adhesion of CHO cells to FN-coated surfaces, indicating that it does not bind to the identified cell-binding domain of FN. A3.3 reacts with a 160/140-kDa doublet, known to contain the cell-binding domain, that is produced by digestion of FN with elastase or thermolysin. However, the antibody does not react with lower molecular weight species that also contain the cell-binding domain or with any of the other identified domains of FN. The A3.3 epitope is extremely protease sensitive and the smallest fragment found in any digest that retains reactivity with A3.3 is a 70-kDa peptide produced in low yield by mild thermolytic cleavage of FN. These data suggest that A3.3 defines a functional site present on both the platelet and plasma FN molecule that has a direct role in platelet aggregation.
1 Communities
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15 MeSH Terms
A monoclonal antibody against human thrombospondin inhibits platelet aggregation.
Dixit VM, Haverstick DM, O'Rourke KM, Hennessy SW, Grant GA, Santoro SA, Frazier WA
(1985) Proc Natl Acad Sci U S A 82: 3472-6
MeSH Terms: Amino Acid Sequence, Antibody Specificity, Blood Platelets, Epitopes, Glycoproteins, Humans, Platelet Aggregation, Serotonin, Thrombospondins
Show Abstract · Added March 5, 2014
A monoclonal antibody (C6.7) has been generated against the calcium-replete form of human platelet thrombospondin (TSP). C6.7 is specific for TSP as determined by both competitive radioimmunoassay and immunoprecipitation. This antibody inhibits both thrombin- and A23187-induced aggregation of gel-filtered platelets in a concentration-dependent manner without affecting the secretion of serotonin. The epitope on TSP recognized by C6.7 has been localized to an 18-kDa fragment that is present in mild chymotryptic digests of TSP. This fragment is disulfide-linked to a 120- to 140-kDa fragment in unreduced digests, and both reduction and denaturation are required to separate the 18-kDa peptide from the larger fragments. A 25-kDa heparin binding domain is also present in the chymotryptic digest. However, the 18-kDa peptide is distinct from the heparin binding domain. The amino acid sequence at the NH2 terminus of the 18-kDa fragment is Asp-Thr-Asn-Pro-Thr-Arg-Ala-Gln-Gly-Tyr-.
1 Communities
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9 MeSH Terms