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Article ; Online: Unconventional viral gene expression mechanisms as therapeutic targets.

Ho, Jessica Sook Yuin / Zhu, Zeyu / Marazzi, Ivan

2021 Volume 593, Issue 7859, Page(s) 362–371

Abstract: Unlike the human genome that comprises mostly noncoding and regulatory sequences, viruses have evolved under the constraints of maintaining a small genome size while expanding the efficiency of their coding and regulatory sequences. As a result, viruses ... ...

Abstract	Unlike the human genome that comprises mostly noncoding and regulatory sequences, viruses have evolved under the constraints of maintaining a small genome size while expanding the efficiency of their coding and regulatory sequences. As a result, viruses use strategies of transcription and translation in which one or more of the steps in the conventional gene-protein production line are altered. These alternative strategies of viral gene expression (also known as gene recoding) can be uniquely brought about by dedicated viral enzymes or by co-opting host factors (known as host dependencies). Targeting these unique enzymatic activities and host factors exposes vulnerabilities of a virus and provides a paradigm for the design of novel antiviral therapies. In this Review, we describe the types and mechanisms of unconventional gene and protein expression in viruses, and provide a perspective on how future basic mechanistic work could inform translational efforts that are aimed at viral eradication.
MeSH term(s)	Animals ; Antiviral Agents/pharmacology ; Antiviral Agents/therapeutic use ; Frameshifting, Ribosomal/drug effects ; Frameshifting, Ribosomal/genetics ; Gene Expression Regulation, Viral/drug effects ; Gene Expression Regulation, Viral/genetics ; Genome, Viral/drug effects ; Genome, Viral/genetics ; Host Microbial Interactions/drug effects ; Host Microbial Interactions/genetics ; Humans ; RNA Splicing/drug effects ; RNA Splicing/genetics ; Virus Diseases/drug therapy ; Virus Diseases/virology
Chemical Substances	Antiviral Agents
Language	English
Publishing date	2021-05-19
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-021-03511-5
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Article ; Online: Generation of host-directed and virus-specific antivirals using targeted protein degradation promoted by small molecules and viral RNA mimics.

Zhao, Nan / Ho, Jessica Sook Yuin / Meng, Fanye / Zheng, Simin / Kurland, Andrew P / Tian, Lu / Rea-Moreno, Martha / Song, Xiangyang / Seo, Ji-Seon / Kaniskan, H Ümit / Te Velthuis, Aartjan J W / Tortorella, Domenico / Chen, Ya-Wen / Johnson, Jeffrey R / Jin, Jian / Marazzi, Ivan

Cell host & microbe

2023 Volume 31, Issue 7, Page(s) 1154–1169.e10

Abstract: Targeted protein degradation (TPD), as exemplified by proteolysis-targeting chimera (PROTAC), is an emerging drug discovery platform. PROTAC molecules, which typically contain a target protein ligand linked to an E3 ligase ligand, recruit a target ... ...

Abstract	Targeted protein degradation (TPD), as exemplified by proteolysis-targeting chimera (PROTAC), is an emerging drug discovery platform. PROTAC molecules, which typically contain a target protein ligand linked to an E3 ligase ligand, recruit a target protein to the E3 ligase to induce its ubiquitination and degradation. Here, we applied PROTAC approaches to develop broad-spectrum antivirals targeting key host factors for many viruses and virus-specific antivirals targeting unique viral proteins. For host-directed antivirals, we identified a small-molecule degrader, FM-74-103, that elicits selective degradation of human GSPT1, a translation termination factor. FM-74-103-mediated GSPT1 degradation inhibits both RNA and DNA viruses. Among virus-specific antivirals, we developed viral RNA oligonucleotide-based bifunctional molecules (Destroyers). As a proof of principle, RNA mimics of viral promoter sequences were used as heterobifunctional molecules to recruit and target influenza viral polymerase for degradation. This work highlights the broad utility of TPD to rationally design and develop next-generation antivirals.
MeSH term(s)	Humans ; Antiviral Agents/pharmacology ; Proteolysis ; RNA, Viral/metabolism ; Ligands ; Viruses/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Viral Proteins/metabolism ; Carrier Proteins/metabolism
Chemical Substances	Antiviral Agents ; RNA, Viral ; Ligands ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Viral Proteins ; Carrier Proteins
Language	English
Publishing date	2023-06-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	2278004-X
ISSN	1934-6069 ; 1931-3128
ISSN (online)	1934-6069
ISSN	1931-3128
DOI	10.1016/j.chom.2023.05.030
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Article ; Online: DNMT3A haploinsufficiency causes dichotomous DNA methylation defects at enhancers in mature human immune cells.

Lim, Jung-Yeon / Duttke, Sascha H / Baker, Turner S / Lee, Jihye / Gambino, Kristyne J / Venturini, Nicholas J / Ho, Jessica Sook Yuin / Zheng, Simin / Fstkchyan, Yesai S / Pillai, Vinodh / Fajgenbaum, David C / Marazzi, Ivan / Benner, Christopher / Byun, Minji

The Journal of experimental medicine

2021 Volume 218, Issue 7

Abstract: DNMT3A encodes an enzyme that carries out de novo DNA methylation, which is essential for the acquisition of cellular identity and specialized functions during cellular differentiation. DNMT3A is the most frequently mutated gene in age-related clonal ... ...

Abstract	DNMT3A encodes an enzyme that carries out de novo DNA methylation, which is essential for the acquisition of cellular identity and specialized functions during cellular differentiation. DNMT3A is the most frequently mutated gene in age-related clonal hematopoiesis. As such, mature immune cells harboring DNMT3A mutations can be readily detected in elderly persons. Most DNMT3A mutations associated with clonal hematopoiesis are heterozygous and predicted to cause loss of function, indicating that haploinsufficiency is the predominant pathogenic mechanism. Yet, the impact of DNMT3A haploinsufficiency on the function of mature immune cells is poorly understood. Here, we demonstrate that DNMT3A haploinsufficiency impairs the gain of DNA methylation at decommissioned enhancers, while simultaneously and unexpectedly impairing DNA demethylation of newly activated enhancers in mature human myeloid cells. The DNA methylation defects alter the activity of affected enhancers, leading to abnormal gene expression and impaired immune response. These findings provide insights into the mechanism of immune dysfunction associated with clonal hematopoiesis and acquired DNMT3A mutations.
MeSH term(s)	Cells, Cultured ; DNA (Cytosine-5-)-Methyltransferases/genetics ; DNA (Cytosine-5-)-Methyltransferases/immunology ; DNA Methylation/genetics ; DNA Methylation/immunology ; DNA Methyltransferase 3A ; Gene Expression/genetics ; Gene Expression/immunology ; Haploinsufficiency/genetics ; Haploinsufficiency/immunology ; Humans ; Immune System/immunology ; Mutation/genetics ; Mutation/immunology ; Regulatory Sequences, Nucleic Acid/genetics ; Regulatory Sequences, Nucleic Acid/immunology
Chemical Substances	DNMT3A protein, human ; DNA (Cytosine-5-)-Methyltransferases (EC 2.1.1.37) ; DNA Methyltransferase 3A (EC 2.1.1.37)
Language	English
Publishing date	2021-05-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	218343-2
ISSN	1540-9538 ; 0022-1007
ISSN (online)	1540-9538
ISSN	0022-1007
DOI	10.1084/jem.20202733
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Article ; Online: Nuclear RNA catabolism controls endogenous retroviruses, gene expression asymmetry, and dedifferentiation.

Torre, Denis / Fstkchyan, Yesai S / Ho, Jessica Sook Yuin / Cheon, Youngseo / Patel, Roosheel S / Degrace, Emma J / Mzoughi, Slim / Schwarz, Megan / Mohammed, Kevin / Seo, Ji-Seon / Romero-Bueno, Raquel / Demircioglu, Deniz / Hasson, Dan / Tang, Weijing / Mahajani, Sameehan U / Campisi, Laura / Zheng, Simin / Song, Won-Suk / Wang, Ying-Chih /

Shah, Hardik / Francoeur, Nancy / Soto, Juan / Salfati, Zelda / Weirauch, Matthew T / Warburton, Peter / Beaumont, Kristin / Smith, Melissa L / Mulder, Lubbertus / Villalta, S Armando / Kessenbrock, Kai / Jang, Cholsoon / Lee, Daeyoup / De Rubeis, Silvia / Cobos, Inma / Tam, Oliver / Hammell, Molly Gale / Seldin, Marcus / Shi, Yongsheng / Basu, Uttiya / Sebastiano, Vittorio / Byun, Minji / Sebra, Robert / Rosenberg, Brad R / Benner, Chris / Guccione, Ernesto / Marazzi, Ivan

Molecular cell

2023 Volume 83, Issue 23, Page(s) 4255–4271.e9

Abstract: Endogenous retroviruses (ERVs) are remnants of ancient parasitic infections and comprise sizable portions of most genomes. Although epigenetic mechanisms silence most ERVs by generating a repressive environment that prevents their expression ( ... ...

Abstract	Endogenous retroviruses (ERVs) are remnants of ancient parasitic infections and comprise sizable portions of most genomes. Although epigenetic mechanisms silence most ERVs by generating a repressive environment that prevents their expression (heterochromatin), little is known about mechanisms silencing ERVs residing in open regions of the genome (euchromatin). This is particularly important during embryonic development, where induction and repression of distinct classes of ERVs occur in short temporal windows. Here, we demonstrate that transcription-associated RNA degradation by the nuclear RNA exosome and Integrator is a regulatory mechanism that controls the productive transcription of most genes and many ERVs involved in preimplantation development. Disrupting nuclear RNA catabolism promotes dedifferentiation to a totipotent-like state characterized by defects in RNAPII elongation and decreased expression of long genes (gene-length asymmetry). Our results indicate that RNA catabolism is a core regulatory module of gene networks that safeguards RNAPII activity, ERV expression, cell identity, and developmental potency.
MeSH term(s)	Endogenous Retroviruses/genetics ; RNA, Nuclear ; Epigenesis, Genetic ; Heterochromatin ; Gene Expression
Chemical Substances	RNA, Nuclear ; Heterochromatin
Language	English
Publishing date	2023-11-22
Publishing country	United States
Document type	Journal Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2023.10.036
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Article ; Online: METTL6 is a tRNA m

Ignatova, Valentina V / Kaiser, Steffen / Ho, Jessica Sook Yuin / Bing, Xinyang / Stolz, Paul / Tan, Ying Xim / Lee, Chee Leng / Gay, Florence Pik Hoon / Lastres, Palma Rico / Gerlini, Raffaele / Rathkolb, Birgit / Aguilar-Pimentel, Antonio / Sanz-Moreno, Adrián / Klein-Rodewald, Tanja / Calzada-Wack, Julia / Ibragimov, Emil / Valenta, Magdalena / Lukauskas, Saulius / Pavesi, Andrea /

Marschall, Susan / Leuchtenberger, Stefanie / Fuchs, Helmut / Gailus-Durner, Valerie / de Angelis, Martin Hrabe / Bultmann, Sebastian / Rando, Oliver J / Guccione, Ernesto / Kellner, Stefanie M / Schneider, Robert

Science advances

2020 Volume 6, Issue 35, Page(s) eaaz4551

Abstract: Recently, covalent modifications of RNA, such as methylation, have emerged as key regulators of all aspects of RNA biology and have been implicated in numerous diseases, for instance, cancer. Here, we undertook a combination of in vitro and in vivo ... ...

Abstract	Recently, covalent modifications of RNA, such as methylation, have emerged as key regulators of all aspects of RNA biology and have been implicated in numerous diseases, for instance, cancer. Here, we undertook a combination of in vitro and in vivo screens to test 78 potential methyltransferases for their roles in hepatocellular carcinoma (HCC) cell proliferation. We identified methyltransferase-like protein 6 (METTL6) as a crucial regulator of tumor cell growth. We show that METTL6 is a bona fide transfer RNA (tRNA) methyltransferase, catalyzing the formation of 3-methylcytidine at C32 of specific serine tRNA isoacceptors. Deletion of
MeSH term(s)	Animals ; Carcinoma, Hepatocellular/genetics ; Cell Proliferation ; Liver Neoplasms/genetics ; Methyltransferases/genetics ; Methyltransferases/metabolism ; Mice ; RNA ; RNA, Transfer/genetics ; RNA, Transfer/metabolism ; tRNA Methyltransferases
Chemical Substances	RNA (63231-63-0) ; RNA, Transfer (9014-25-9) ; METTL6 protein, human (EC 2.1.1.-) ; Methyltransferases (EC 2.1.1.-) ; tRNA Methyltransferases (EC 2.1.1.-)
Language	English
Publishing date	2020-08-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.aaz4551
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Article: Topoisomerase 1 inhibition therapy protects against SARS-CoV-2-induced inflammation and death in animal models.

Yuin Ho, Jessica Sook / Wing-Yee Mok, Bobo / Campisi, Laura / Jordan, Tristan / Yildiz, Soner / Parameswaran, Sreeja / Wayman, Joseph A / Gaudreault, Natasha N / Meekins, David A / Indran, Sabarish V / Morozov, Igor / Trujillo, Jessie D / Fstkchyan, Yesai S / Rathnasinghe, Raveen / Zhu, Zeyu / Zheng, Simin / Zhao, Nan / White, Kris / Ray-Jones, Helen /

Malysheva, Valeriya / Thiecke, Michiel J / Lau, Siu-Ying / Liu, Honglian / Junxia Zhang, Anna / Chak-Yiu Lee, Andrew / Liu, Wen-Chun / Aydillo, Teresa / Salom Melo, Betsaida / Guccione, Ernesto / Sebra, Robert / Shum, Elaine / Bakker, Jan / Kaufman, David A / Moreira, Andre L / Carossino, Mariano / Balasuriya, Udeni B R / Byun, Minji / Miraldi, Emily R / Albrecht, Randy A / Schotsaert, Michael / Garcia-Sastre, Adolfo / Chanda, Sumit K / Jeyasekharan, Anand D / TenOever, Benjamin R / Spivakov, Mikhail / Weirauch, Matthew T / Heinz, Sven / Chen, Honglin / Benner, Christopher / Richt, Juergen A / Marazzi, Ivan

bioRxiv : the preprint server for biology

2020

Abstract: The ongoing pandemic caused by Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) is currently affecting millions of lives worldwide. Large retrospective studies indicate that an elevated level of inflammatory cytokines and pro-inflammatory ... ...

Abstract	The ongoing pandemic caused by Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) is currently affecting millions of lives worldwide. Large retrospective studies indicate that an elevated level of inflammatory cytokines and pro-inflammatory factors are associated with both increased disease severity and mortality. Here, using multidimensional epigenetic, transcriptional,
Language	English
Publishing date	2020-12-01
Publishing country	United States
Document type	Preprint
DOI	10.1101/2020.12.01.404483
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Article ; Online: Discovery of a chemical probe for PRDM9

Abdellah Allali-Hassani / Magdalena M. Szewczyk / Danton Ivanochko / Shawna L. Organ / Jabez Bok / Jessica Sook Yuin Ho / Florence P. H. Gay / Fengling Li / Levi Blazer / Mohammad S. Eram / Levon Halabelian / David Dilworth / Genna M. Luciani / Evelyne Lima-Fernandes / Qin Wu / Peter Loppnau / Nathan Palmer / S. Zakiah A. Talib / Peter J. Brown /

Matthieu Schapira / Philipp Kaldis / Ronan C. O’Hagan / Ernesto Guccione / Dalia Barsyte-Lovejoy / Cheryl H. Arrowsmith / John M. Sanders / Solomon D. Kattar / D. Jonathan Bennett / Benjamin Nicholson / Masoud Vedadi

Nature Communications, Vol 10, Iss 1, Pp 1-

2019 Volume 11

Abstract: PRDM9 is a PR domain containing histone methyl transferase which expression is normally restricted to the germline that has also been linked to a number of somatic cancers. Here the authors describe the identification of a small molecule that selectivity ...

Abstract	PRDM9 is a PR domain containing histone methyl transferase which expression is normally restricted to the germline that has also been linked to a number of somatic cancers. Here the authors describe the identification of a small molecule that selectivity inhibits the methyltransferase activity of PRDM9 in biochemical and cellular assays
Keywords	Science ; Q
Language	English
Publishing date	2019-12-01T00:00:00Z
Publisher	Nature Publishing Group
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Discovery of a chemical probe for PRDM9

Nature Communications, Vol 10, Iss 1, Pp 1-

2019 Volume 11

Abstract	PRDM9 is a PR domain containing histone methyl transferase which expression is normally restricted to the germline that has also been linked to a number of somatic cancers. Here the authors describe the identification of a small molecule that selectivity inhibits the methyltransferase activity of PRDM9 in biochemical and cellular assays
Keywords	Science ; Q
Language	English
Publishing date	2019-12-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Discovery of a chemical probe for PRDM9.

Allali-Hassani, Abdellah / Szewczyk, Magdalena M / Ivanochko, Danton / Organ, Shawna L / Bok, Jabez / Ho, Jessica Sook Yuin / Gay, Florence P H / Li, Fengling / Blazer, Levi / Eram, Mohammad S / Halabelian, Levon / Dilworth, David / Luciani, Genna M / Lima-Fernandes, Evelyne / Wu, Qin / Loppnau, Peter / Palmer, Nathan / Talib, S Zakiah A / Brown, Peter J /

Schapira, Matthieu / Kaldis, Philipp / O'Hagan, Ronan C / Guccione, Ernesto / Barsyte-Lovejoy, Dalia / Arrowsmith, Cheryl H / Sanders, John M / Kattar, Solomon D / Bennett, D Jonathan / Nicholson, Benjamin / Vedadi, Masoud

Nature communications

2019 Volume 10, Issue 1, Page(s) 5759

Abstract: PRDM9 is a PR domain containing protein which trimethylates histone 3 on lysine 4 and 36. Its normal expression is restricted to germ cells and attenuation of its activity results in altered meiotic gene transcription, impairment of double-stranded ... ...

Abstract	PRDM9 is a PR domain containing protein which trimethylates histone 3 on lysine 4 and 36. Its normal expression is restricted to germ cells and attenuation of its activity results in altered meiotic gene transcription, impairment of double-stranded breaks and pairing between homologous chromosomes. There is growing evidence for a role of aberrant expression of PRDM9 in oncogenesis and genome instability. Here we report the discovery of MRK-740, a potent (IC
MeSH term(s)	Crystallography, X-Ray ; DNA Methylation/drug effects ; Drug Discovery/methods ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; HEK293 Cells ; Histone-Lysine N-Methyltransferase/antagonists & inhibitors ; Histone-Lysine N-Methyltransferase/metabolism ; Histone-Lysine N-Methyltransferase/ultrastructure ; Histones/metabolism ; Humans ; Inhibitory Concentration 50 ; Molecular Dynamics Simulation ; Molecular Probes/chemistry ; Molecular Probes/pharmacology ; Protein Domains ; S-Adenosylmethionine/metabolism
Chemical Substances	Enzyme Inhibitors ; Histones ; Molecular Probes ; histone H3 trimethyl Lys4 ; S-Adenosylmethionine (7LP2MPO46S) ; Histone-Lysine N-Methyltransferase (EC 2.1.1.43) ; PRDM9 protein, human (EC 2.1.1.43)
Language	English
Publishing date	2019-12-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-019-13652-x
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Article ; Online: TOP1 inhibition therapy protects against SARS-CoV-2-induced lethal inflammation.

Ho, Jessica Sook Yuin / Mok, Bobo Wing-Yee / Campisi, Laura / Jordan, Tristan / Yildiz, Soner / Parameswaran, Sreeja / Wayman, Joseph A / Gaudreault, Natasha N / Meekins, David A / Indran, Sabarish V / Morozov, Igor / Trujillo, Jessie D / Fstkchyan, Yesai S / Rathnasinghe, Raveen / Zhu, Zeyu / Zheng, Simin / Zhao, Nan / White, Kris / Ray-Jones, Helen /

Malysheva, Valeriya / Thiecke, Michiel J / Lau, Siu-Ying / Liu, Honglian / Zhang, Anna Junxia / Lee, Andrew Chak-Yiu / Liu, Wen-Chun / Jangra, Sonia / Escalera, Alba / Aydillo, Teresa / Melo, Betsaida Salom / Guccione, Ernesto / Sebra, Robert / Shum, Elaine / Bakker, Jan / Kaufman, David A / Moreira, Andre L / Carossino, Mariano / Balasuriya, Udeni B R / Byun, Minji / Albrecht, Randy A / Schotsaert, Michael / Garcia-Sastre, Adolfo / Chanda, Sumit K / Miraldi, Emily R / Jeyasekharan, Anand D / TenOever, Benjamin R / Spivakov, Mikhail / Weirauch, Matthew T / Heinz, Sven / Chen, Honglin / Benner, Christopher / Richt, Juergen A / Marazzi, Ivan

Cell

2021 Volume 184, Issue 10, Page(s) 2618–2632.e17

Abstract: The ongoing pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is currently affecting millions of lives worldwide. Large retrospective studies indicate that an elevated level of inflammatory cytokines and pro-inflammatory ... ...

Abstract	The ongoing pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is currently affecting millions of lives worldwide. Large retrospective studies indicate that an elevated level of inflammatory cytokines and pro-inflammatory factors are associated with both increased disease severity and mortality. Here, using multidimensional epigenetic, transcriptional, in vitro, and in vivo analyses, we report that topoisomerase 1 (TOP1) inhibition suppresses lethal inflammation induced by SARS-CoV-2. Therapeutic treatment with two doses of topotecan (TPT), an FDA-approved TOP1 inhibitor, suppresses infection-induced inflammation in hamsters. TPT treatment as late as 4 days post-infection reduces morbidity and rescues mortality in a transgenic mouse model. These results support the potential of TOP1 inhibition as an effective host-directed therapy against severe SARS-CoV-2 infection. TPT and its derivatives are inexpensive clinical-grade inhibitors available in most countries. Clinical trials are needed to evaluate the efficacy of repurposing TOP1 inhibitors for severe coronavirus disease 2019 (COVID-19) in humans.
MeSH term(s)	Animals ; COVID-19/enzymology ; COVID-19/pathology ; Chlorocebus aethiops ; DNA Topoisomerases, Type I/metabolism ; Humans ; Inflammation/drug therapy ; Inflammation/enzymology ; Inflammation/pathology ; Inflammation/virology ; Mesocricetus ; Mice ; Mice, Transgenic ; SARS-CoV-2/metabolism ; THP-1 Cells ; Topoisomerase I Inhibitors/pharmacology ; Topotecan/pharmacology ; Vero Cells ; COVID-19 Drug Treatment
Chemical Substances	Topoisomerase I Inhibitors ; Topotecan (7M7YKX2N15) ; DNA Topoisomerases, Type I (EC 5.99.1.2) ; TOP1 protein, human (EC 5.99.1.2)
Language	English
Publishing date	2021-03-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2021.03.051
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