ORCID Profile
0000-0001-6005-0016
Current Organisation
Fred Hutchinson Cancer Research Center
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Publisher: Royal Society of Chemistry (RSC)
Date: 2018
DOI: 10.1039/C8CC90189A
Abstract: For the third time, a Faraday Discussion addressed ionic liquids. Encompassing the wealth of research in this field, the contributions ranged from fundamental insights to the erse applications of ionic liquids. Lively discussions initiated in the lecture hall and during poster sessions then seamlessly continued during the social program.
Publisher: Public Library of Science (PLoS)
Date: 04-12-2009
Publisher: Springer Science and Business Media LLC
Date: 31-05-2012
Abstract: Histone variants are non-allelic protein isoforms that play key roles in ersifying chromatin structure. The known number of such variants has greatly increased in recent years, but the lack of naming conventions for them has led to a variety of naming styles, multiple synonyms and misleading homographs that obscure variant relationships and complicate database searches. We propose here a unified nomenclature for variants of all five classes of histones that uses consistent but flexible naming conventions to produce names that are informative and readily searchable. The nomenclature builds on historical usage and incorporates phylogenetic relationships, which are strong predictors of structure and function. A key feature is the consistent use of punctuation to represent phylogenetic ergence, making explicit the relationships among variant subtypes that have previously been implicit or unclear. We recommend that by default new histone variants be named with organism-specific paralog-number suffixes that lack phylogenetic implication, while letter suffixes be reserved for structurally distinct clades of variants. For clarity and searchability, we encourage the use of descriptors that are separate from the phylogeny-based variant name to indicate developmental and other properties of variants that may be independent of structure.
Publisher: Cold Spring Harbor Laboratory
Date: 22-03-2020
DOI: 10.1101/2020.03.22.002386
Abstract: An outbreak of the novel coronavirus SARS-CoV-2, the causative agent of COVID-19 respiratory disease, has infected over 290,000 people since the end of 2019, killed over 12,000, and caused worldwide social and economic disruption 1,2 . There are currently no antiviral drugs with proven efficacy nor are there vaccines for its prevention. Unfortunately, the scientific community has little knowledge of the molecular details of SARS-CoV-2 infection. To illuminate this, we cloned, tagged and expressed 26 of the 29 viral proteins in human cells and identified the human proteins physically associated with each using affinity-purification mass spectrometry (AP-MS), which identified 332 high confidence SARS-CoV-2-human protein-protein interactions (PPIs). Among these, we identify 66 druggable human proteins or host factors targeted by 69 existing FDA-approved drugs, drugs in clinical trials and/or preclinical compounds, that we are currently evaluating for efficacy in live SARS-CoV-2 infection assays. The identification of host dependency factors mediating virus infection may provide key insights into effective molecular targets for developing broadly acting antiviral therapeutics against SARS-CoV-2 and other deadly coronavirus strains.
Publisher: Springer Science and Business Media LLC
Date: 30-04-2010
Location: United States of America
No related grants have been discovered for Harmit Malik.