Matthew D. Scharff

ORCID: 0000-0003-0368-2433
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About
Contact & Profiles
Research Areas
  • Monoclonal and Polyclonal Antibodies Research
  • T-cell and B-cell Immunology
  • Glycosylation and Glycoproteins Research
  • Protein purification and stability
  • Fungal Infections and Studies
  • Immune Cell Function and Interaction
  • DNA Repair Mechanisms
  • Chronic Lymphocytic Leukemia Research
  • Immunodeficiency and Autoimmune Disorders
  • Genetic factors in colorectal cancer
  • Viral Infectious Diseases and Gene Expression in Insects
  • Toxin Mechanisms and Immunotoxins
  • RNA and protein synthesis mechanisms
  • Antifungal resistance and susceptibility
  • Multiple Myeloma Research and Treatments
  • Virus-based gene therapy research
  • Nail Diseases and Treatments
  • Bacteriophages and microbial interactions
  • CRISPR and Genetic Engineering
  • Cancer Genomics and Diagnostics
  • Transgenic Plants and Applications
  • Immunotherapy and Immune Responses
  • Galectins and Cancer Biology
  • Lymphoma Diagnosis and Treatment
  • CAR-T cell therapy research

Albert Einstein College of Medicine
2013-2025

Office of Infectious Diseases
1995-2010

Yeshiva University
1986-2009

University of New Brunswick
2005

University of Southern California
2001-2005

University of Toronto
2005

Bipar
2005

Rockefeller University
1998

National Institutes of Health
1963-1996

Rappaport Family Institute for Research in the Medical Sciences
1988-1994

The expression of activation-induced cytidine deaminase (AID) is prerequisite to a “trifecta” key molecular events in B cells: class-switch recombination and somatic hypermutation humans mice gene conversion chickens. Although this critically important enzyme shares common sequence motifs with apolipoprotein mRNA-editing enzyme, exhibits activity on free deoxycytidine solution, it has not been shown act either RNA or DNA. Recent mutagenesis data Escherichia coli suggest that AID may...

10.1073/pnas.0730835100 article EN Proceedings of the National Academy of Sciences 2003-03-21

The S107 IgA kappa-chain myeloma cell line makes an antiphosphocholine antibody of the T15 idiotype. A somatic mutant this line, U4, immunoglobulin with a single amino acid substitution alanine for glutamic at residue 35. This change results in loss phosphocholine binding activity. However, U4 has acquired reactivity variety phosphorylated macromolecules, including double-stranded DNA, protamine, and cardiolipin. Thus, heavy chain can transform antibacterial into that resembles...

10.1073/pnas.81.18.5841 article EN Proceedings of the National Academy of Sciences 1984-09-01

MPC-11 myeloma tumor cells were adapted to growth in continuous culture. The cultured resembled the parent that they produced fully assembled gamma globulin molecules as well six unassembled molecules. Although and synthesized excess light chains, molar ratio of (L) heavy (H) chains was approximately 1.7:1 culture, 3.5:1 tumor. also fewer half free than Peptide column analysis did not reveal differences primary structure H derived from L may have differed by a minor peptide. As much 20%...

10.1084/jem.131.3.515 article EN The Journal of Experimental Medicine 1970-03-01

ABSTRACT The murine monoclonal antibody (MAb) 18B7 [immunoglobulin G1(κ)] is in preclinical development for treatment of Cryptococcus neoformans infections. In anticipation its use humans, we defined the serological and biological properties MAb detail. Structural comparison to related protective 2H1 revealed conservation antigen binding site despite several amino acid differences. was shown by immunofluorescence agglutination studies bind all four serotypes C. , opsonize A D, enhance human...

10.1128/aac.42.6.1437 article EN Antimicrobial Agents and Chemotherapy 1998-06-01

Several murine monoclonal antibodies (MAbs) specific for the capsular glucuronoxylomannan of Cryptococcus neoformans were studied their capacity to confer protection when passively administered lethally infected mice. The MAb group recognized at least three distinct epitopes and included immunoglobulin M (IgM), IgG3, IgG1, IgA isotypes. model used A/J BALB/c mice intraperitoneally with 10(8) cryptococci. MAbs either immediately preceding or, in one experiment, 24 48 h prior infection....

10.1128/iai.60.11.4534-4541.1992 article EN Infection and Immunity 1992-11-01

Rat monoclonal antibodies specific for mouse kappa light chains and γ heavy have been generated. These rat biosynthetically labelled with 35S methionine. The free label was dialyzed from the medium and, without further purification, containing radioactive antibody used in a radioimmunoassay to screen sera of immunized animals hybridomas IgG class.

10.1089/hyb.1.1981.1.5 article EN Hybridoma 1981-01-01

Abstract Cultured mouse myeloma cells have been cloned in soft agar using a modification of the method established by Pluznik and Sachs ('65, '66) Bradley Metcalf ('66). A linear relationship existed between number plated colonies produced. Conditions for obtaining optimum cloning efficiency colony size were determined MPC‐11 cell line. Feeder mouse, human rabbit origin conditioned growth medium obtained from cultures had an enhancing effect on formation. Immunoglobulin production was...

10.1002/jcp.1040790313 article EN Journal of Cellular Physiology 1972-06-01

Cultures of mouse myeloma cells which secrete both heavy (H) and light (L) immunoglobulin chains were cloned in soft agar. Variants that synthesized neither chain, or only chains, detected by overlaying the growing colonies with antiserum specific for individual chains. The rate conversion plus chain producers to was 1.1 x 10(-3) per cell generation, as determined fluctuation analysis.

10.1073/pnas.68.1.219 article EN Proceedings of the National Academy of Sciences 1971-01-01

10.1016/0005-2787(67)90715-0 article EN Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis 1967-11-01

Although the primary function of DNA mismatch repair (MMR) system is to identify and correct base mismatches that have been erroneously introduced during replication, recent studies further implicated several MMR components in somatic hypermutation immunoglobulin (Ig) genes. We studied immune response mice deficient MutS homologue (MSH)3 MSH6, two mutually exclusive partners MSH2 not examined previously for their role Ig hypermutation. In Msh6−/− Msh3−/−/Msh6−/− mice, substitutions are...

10.1084/jem.191.3.579 article EN The Journal of Experimental Medicine 2000-02-07

Two immunoglobulin M monoclonal antibodies (mAbs) derived from the same B cell recognize different epitopes on capsular polysaccharide of pathogenic yeast, Cryptococcus neoformans. Their respective are located in spatially distinct regions capsule. Passive administration one mAb prolonged survival whereas other did not. The results indicate that specificity is an important determinant antibody efficacy against C. neoformans and somatic mutations occurring during response can affect protective to

10.1084/jem.181.1.405 article EN The Journal of Experimental Medicine 1995-01-01

T-cell costimulation and coinhibition generated by engagement of the B7 family their receptor CD28 are central importance in regulating response, making these pathways very attractive therapeutic targets. Here we describe HERV–H LTR-associating protein 2 (HHLA2) as a member that shares 10–18% amino acid identity 23–33% similarity to other human proteins phylogenetically forms subfamily with B7x B7-H3 within family. HHLA2 is expressed humans but not mice, which unique families. constitutively...

10.1073/pnas.1303524110 article EN Proceedings of the National Academy of Sciences 2013-05-28

Antibodies to double-stranded DNA are pathognomonic of systemic lupus erythematosus and deposit in the kidneys patients cause glomerulonephritis. Recent data suggest that a significant proportion anti-DNA antibodies may cross-react with renal antigens be sequestered kidney by virtue this cross-reactivity. If is true, antigenic competition for pathogenic might prevent their deposition ensuing tissue damage. To generate surrogate could used purpose, we have peptide display phage libraries...

10.1073/pnas.94.5.1955 article EN Proceedings of the National Academy of Sciences 1997-03-04
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