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Mark M. Davis

Researcher at Stanford University

Publications -  623
Citations -  84251

Mark M. Davis is an academic researcher from Stanford University. The author has contributed to research in topics: T cell & T-cell receptor. The author has an hindex of 144, co-authored 581 publications receiving 74358 citations. Previous affiliations of Mark M. Davis include Washington University in St. Louis & University of Chicago.

Papers
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Posted ContentDOI

CD38 contributes to human natural killer cell responses through a role in immune synapse formation

TL;DR: It is demonstrated that the cell surface protein CD38 is a key human NK cell functional receptor through a role in immune synapse formation and opens new avenues in immunotherapeutic development for cancer and infection by revealing a critical role for CD38 in NK cell function.
Posted ContentDOI

Multiomic Immunophenotyping of COVID-19 Patients Reveals Early Infection Trajectories.

TL;DR: A comprehensive immune response map spanning 454 proteins and 847 metabolites in plasma integrated with single-cell multi-omic assays of PBMCs is presented in which whole transcriptome, 192 surface proteins, and T and B cell receptor sequence were co-analyzed within the context of clinical measures from 50 COVID19 patient samples.
Journal ArticleDOI

The Stanford Data Miner: a novel approach for integrating and exploring heterogeneous immunological data

TL;DR: The tools and techniques of data warehousing, including open-source business intelligence software, are used to support investigator-driven data integration and mining of diverse immunological data and can be used to find gender-specific differences in serum cytokine levels.
Patent

Cadherin-like asymmetry protein-1, and methods for its use

TL;DR: In this article, a cell surface protein which contains certain classical cadherin characteristics, but exhibits an apical distribution pattern on the surface of lymphocytes, is described and the membrane location correlates with the contact interface between T and B cells, and antibodies against an extracellular domain of this protein disrupt T cell/B cell interactions.