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Catharina C. Gross

Researcher at University of Münster

Publications -  145
Citations -  5547

Catharina C. Gross is an academic researcher from University of Münster. The author has contributed to research in topics: Multiple sclerosis & Immune system. The author has an hindex of 35, co-authored 119 publications receiving 4184 citations. Previous affiliations of Catharina C. Gross include University Hospital Regensburg & National Institutes of Health.

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Heat shock protein 70 surface-positive tumor exosomes stimulate migratory and cytolytic activity of natural killer cells

TL;DR: The data provide an explanation how Hsp70 reactivity in NK cells is induced by tumor-derived exosomes, and the exosome-mediated lytic activity of NK cells was blockable by HSp70-specific antibody.
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Treatment of colon and lung cancer patients with ex vivo heat shock protein 70-peptide-activated, autologous natural killer cells: a clinical phase i trial.

TL;DR: Immunological results warrant additional studies in patients with lower tumor burden, and reinfusion of Hsp70-activated autologous NK cells is safe, and cytolytic activity of NK cells against HSP70 membrane-positive colon carcinoma cells was enhanced after TKD/IL-2 stimulation.
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Integrated single cell analysis of blood and cerebrospinal fluid leukocytes in multiple sclerosis

TL;DR: A single-cell characterization of cerebrospinal fluid and blood of newly diagnosed multiple sclerosis patients is provided, revealing altered composition of lymphocyte and monocyte subsets, validated by other methods including the interrogation of the TFH subset in mouse models of MS.
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A 14-mer Hsp70 peptide stimulates natural killer (NK) cell activity

TL;DR: Most interestingly, similar to full-length Hsp70 protein, the N-terminal–extended 14-mer peptide TKDNNLLGRFELSG (TKD, aa 450–463) was able to stimulate the cytolytic and proliferative activity of NK cells at concentrations equivalent to full -length HSp70 protein.
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Cell Surface-bound Heat Shock Protein 70 (Hsp70) Mediates Perforin-independent Apoptosis by Specific Binding and Uptake of Granzyme B

TL;DR: A novel perforin-independent, granzyme B-mediated apoptosis pathway for Hsp70 membrane-positive tumor cells is proposed by affinity chromatography that specifically bind a 32-kDa protein derived from NK cell lysates.