Michael Reth

ORCID: 0000-0002-1025-7198
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About
Contact & Profiles
Research Areas
  • T-cell and B-cell Immunology
  • Immune Cell Function and Interaction
  • Monoclonal and Polyclonal Antibodies Research
  • Immunotherapy and Immune Responses
  • Glycosylation and Glycoproteins Research
  • Cell Adhesion Molecules Research
  • Immunodeficiency and Autoimmune Disorders
  • Mycobacterium research and diagnosis
  • Chronic Lymphocytic Leukemia Research
  • Immune Response and Inflammation
  • CAR-T cell therapy research
  • Galectins and Cancer Biology
  • Viral Infectious Diseases and Gene Expression in Insects
  • NF-κB Signaling Pathways
  • Calcium signaling and nucleotide metabolism
  • Toxin Mechanisms and Immunotoxins
  • PI3K/AKT/mTOR signaling in cancer
  • Protein Tyrosine Phosphatases
  • HIV Research and Treatment
  • Protein Kinase Regulation and GTPase Signaling
  • Erythrocyte Function and Pathophysiology
  • Lipid Membrane Structure and Behavior
  • Adenosine and Purinergic Signaling
  • Epigenetics and DNA Methylation
  • CRISPR and Genetic Engineering

University of Freiburg
2015-2024

University Medical Center Freiburg
2015-2024

TU Bergakademie Freiberg
2021

Max Planck Institute of Immunobiology and Epigenetics
2010-2019

University of Cologne
1981-2015

Centre for Chronic Disease Control
2015

Institute of Molecular Medicine
2015

Max Planck Society
2002-2014

Boston Children's Hospital
2014

Harvard University
2014

The mb1 gene encodes the Ig-α signaling subunit of B cell antigen receptor and is expressed exclusively in cells beginning at very early pro-B stage bone marrow. We examine here efficacy as a host locus for cre recombinase expression cells. show that by integrating humanized into we obtain extraordinarily efficient recombination loxP sites lineage. results from variety reporter genes including splicing factor SRp20 DNA methylase Dnmt1 suggest mb1-cre probably best model so far described...

10.1073/pnas.0605944103 article EN Proceedings of the National Academy of Sciences 2006-08-30

Abstract Spleen cells from C57BL/6 mice sensitized to the hapten (4‐hydroxy‐3‐nitrophenyl)acetyl (NP) were hybridized with myeloma cells, and a variety of hybrid cell lines was isolated which secreted homogeneous anti‐NP antibodies. The antibodies purified by affinity chromatography their chain composition, fine specificity determined. All recovered primary immune response carried λ light μ or γ 1 heavy chains. Their variable portions nonidentical but similar in terms hapten‐binding higher...

10.1002/eji.1830080605 article EN European Journal of Immunology 1978-06-01

During signal transduction through the B cell antigen receptor (BCR), several signaling elements are brought together by adaptor protein SLP-65. We have investigated role of SLP-65 in maturation and function mice deficient for While viable, development is affected at stages. SLP-65-deficient show increased proportions pre-B cells bone marrow immature peripheral lymphoid organs. B1 lacking. The lower IgM IgG3 serum titers poor but normal IgG immune responses. Mutant reduced Ca2+ mobilization...

10.1016/s1074-7613(00)80130-2 article EN cc-by-nc-nd Immunity 1999-11-01

The immunoglobulin α (Ig-α)-Ig-β heterodimer is the signaling component of antigen receptor complex on B cells (BCR) and cell progenitors (pre-BCR). A mouse mutant that lacks most Ig-α cytoplasmic tail exhibits only a small impairment in early development but severe block generation peripheral pool, revealing checkpoint maturation ensures expression functional BCR mature cells. do develop demonstrate differential dependence antibody responses such signaling-competent appears to be critical...

10.1126/science.272.5269.1804 article EN Science 1996-06-21

The site-directed recombinase Cre can be employed to delete or express genes in cell lines animals. Clearly, the ability control remotely activity of this enzyme would highly desirable. To end we have constructed expression vectors for fusion proteins consisting and a mutated hormone-binding domain murine oestrogen receptor. latter still binds anti-oestrogen drug tamoxifen but no longer 17β-oestradiol. We show here that embryonic stem cells expressing such proteins, efficiently induce...

10.1093/nar/24.4.543 article EN Nucleic Acids Research 1996-02-01

The current structural model of the B cell antigen receptor (BCR) describes it as a symmetric protein complex in which one membrane-bound immunoglobulin molecule (mIg) is noncovalently bound on each side by an Ig-alpha/Ig-beta heterodimer. Using peptide-tagged Ig-alpha proteins, blue native polyacrylamide gel electrophoresis (BN-PAGE), and biosynthetical labeling cells, we find that mIg:Ig-alpha/Ig-beta has stoichiometry 1:1 not 1:2. An anti-Flag stimulation cells coexpressing Flag-tagged...

10.1016/s1074-7613(00)00003-0 article EN cc-by-nc-nd Immunity 2000-07-01

The B cell antigen receptor (BCR) consists of the membrane-bound immunoglobulin (Ig) molecule as antigen-binding subunit and Ig-α/Ig-β heterodimer signaling subunit. BCR signal transduction involves activation protein tyrosine kinases (PTKs) phosphorylation several proteins, only some which have been identified. these proteins can be induced by exposure cells either to or phosphatase inhibitor pervanadate/H2O2. One earliest substrates in is a 65-kD protein, we identify here adaptor protein....

10.1084/jem.188.4.791 article EN The Journal of Experimental Medicine 1998-08-17
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