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Coordinating cell cycle-regulated histone gene expression through assembly and function of the Histone Locus Body

RNA biology, 2017-06, Vol.14 (6), p.726-738

2017

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Structure of an active human histone pre-mRNA 3'-end processing machinery

Science (American Association for the Advancement of Science), 2020-02, Vol.367 (6478), p.700-703

2020

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Concentrating pre-mRNA processing factors in the histone locus body facilitates efficient histone mRNA biogenesis

The Journal of cell biology, 2016-06, Vol.213 (5), p.557-570

2016

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Protein composition of catalytically active U7-dependent processing complexes assembled on histone pre-mRNA containing biotin and a photo-cleavable linker

Nucleic acids research, 2018-05, Vol.46 (9), p.4752-4770

2018

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A Core Complex of CPSF73, CPSF100, and Symplekin May Form Two Different Cleavage Factors for Processing of Poly(A) and Histone mRNAs

Molecular cell, 2009-05, Vol.34 (3), p.322-332

2009

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FLASH, a Proapoptotic Protein Involved in Activation of Caspase-8, Is Essential for 3′ End Processing of Histone Pre-mRNAs

Molecular cell, 2009-10, Vol.36 (2), p.267-278

2009

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The Polyadenylation Factor CPSF-73 Is Involved in Histone-Pre-mRNA Processing

Cell, 2005-10, Vol.123 (1), p.37-48

2005

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The N-terminal domains of FLASH and Lsm11 form a 2:1 heterotrimer for histone pre-mRNA 3'-end processing

PloS one, 2017-10, Vol.12 (10), p.e0186034-e0186034

2017

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A Complex Containing the CPSF73 Endonuclease and Other Polyadenylation Factors Associates with U7 snRNP and Is Recruited to Histone Pre-mRNA for 3′-End Processing

Molecular and Cellular Biology, 2013-01, Vol.33 (1), p.28-37

2013

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Mapping the Interaction Network of Key Proteins Involved in Histone mRNA Generation: A Hydrogen/Deuterium Exchange Study

Journal of molecular biology, 2016-03, Vol.428 (6), p.1180-1196

2016

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Drosophila histone locus bodies form by hierarchical recruitment of components

The Journal of cell biology, 2011-05, Vol.193 (4), p.677-694

2011

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Studies of the 5′ Exonuclease and Endonuclease Activities of CPSF-73 in Histone Pre-mRNA Processing

Molecular and Cellular Biology, 2009-01, Vol.29 (1), p.31-42

2009

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Interaction between FLASH and Lsm11 is essential for histone pre-mRNA processing in vivo in Drosophila

RNA (Cambridge), 2011-06, Vol.17 (6), p.1132-1147

2011

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FLASH Is Required for the Endonucleolytic Cleavage of Histone Pre-mRNAs but Is Dispensable for the 5′ Exonucleolytic Degradation of the Downstream Cleavage Product

Molecular and Cellular Biology, 2011-04, Vol.31 (7), p.1492-1502

2011

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Cell cycle-regulated protein abundance changes in synchronously proliferating HeLa cells include regulation of pre-mRNA splicing proteins

PloS one, 2013-03, Vol.8 (3), p.e58456-e58456

2013

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Three Proteins of the U7-Specific Sm Ring Function as the Molecular Ruler To Determine the Site of 3′-End Processing in Mammalian Histone Pre-mRNA

Molecular and Cellular Biology, 2009-08, Vol.29 (15), p.4045-4056

2009

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ZFP100, a Component of the Active U7 snRNP Limiting for Histone Pre-mRNA Processing, Is Required for Entry into S Phase

Molecular and Cellular Biology, 2006-09, Vol.26 (17), p.6702-6712

2006

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Reconstitution and biochemical assays of an active human histone pre-mRNA 3'-end processing machinery

Methods in enzymology, 2021, Vol.655, p.291-324

2021

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Developmental Control of Histone mRNA and dSLBP Synthesis during Drosophila Embryogenesis and the Role of dSLBP in Histone mRNA 3′ End Processing In Vivo

Molecular and Cellular Biology, 2002-04, Vol.22 (7), p.2267-2282

2002

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U7 snRNP is recruited to histone pre-mRNA in a FLASH-dependent manner by two separate regions of the stem-loop binding protein

RNA (Cambridge), 2017-06, Vol.23 (6), p.938-951

2017

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3'-End processing of histone pre-mRNAs in Drosophila: U7 snRNP is associated with FLASH and polyadenylation factors

RNA (Cambridge), 2013-12, Vol.19 (12), p.1726-1744

2013

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Histone mRNA expression: multiple levels of cell cycle regulation and important developmental consequences

Current Opinion in Cell Biology, 2002-12, Vol.14 (6), p.692-699

2002

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U7 snRNA mutations in Drosophila block histone pre-mRNA processing and disrupt oogenesis

RNA (Cambridge), 2006-03, Vol.12 (3), p.396-409

2006

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More than one way to make a tail

The EMBO journal, 2010-12, Vol.29 (24), p.4066-4067

Marzluff, William F

2010

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Formation of the 3′ end of histone mRNA

Gene, 1999-10, Vol.239 (1), p.1-14

1999

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Coordinating cell cycle-regulated histone gene expression through assembly and function of the Histone Locus Body

Structure of an active human histone pre-mRNA 3'-end processing machinery

Concentrating pre-mRNA processing factors in the histone locus body facilitates efficient histone mRNA biogenesis

Protein composition of catalytically active U7-dependent processing complexes assembled on histone pre-mRNA containing biotin and a photo-cleavable linker

A Core Complex of CPSF73, CPSF100, and Symplekin May Form Two Different Cleavage Factors for Processing of Poly(A) and Histone mRNAs

FLASH, a Proapoptotic Protein Involved in Activation of Caspase-8, Is Essential for 3′ End Processing of Histone Pre-mRNAs

The Polyadenylation Factor CPSF-73 Is Involved in Histone-Pre-mRNA Processing

The N-terminal domains of FLASH and Lsm11 form a 2:1 heterotrimer for histone pre-mRNA 3'-end processing

A Complex Containing the CPSF73 Endonuclease and Other Polyadenylation Factors Associates with U7 snRNP and Is Recruited to Histone Pre-mRNA for 3′-End Processing

Mapping the Interaction Network of Key Proteins Involved in Histone mRNA Generation: A Hydrogen/Deuterium Exchange Study

Drosophila histone locus bodies form by hierarchical recruitment of components

Studies of the 5′ Exonuclease and Endonuclease Activities of CPSF-73 in Histone Pre-mRNA Processing

Interaction between FLASH and Lsm11 is essential for histone pre-mRNA processing in vivo in Drosophila

FLASH Is Required for the Endonucleolytic Cleavage of Histone Pre-mRNAs but Is Dispensable for the 5′ Exonucleolytic Degradation of the Downstream Cleavage Product

Cell cycle-regulated protein abundance changes in synchronously proliferating HeLa cells include regulation of pre-mRNA splicing proteins

Three Proteins of the U7-Specific Sm Ring Function as the Molecular Ruler To Determine the Site of 3′-End Processing in Mammalian Histone Pre-mRNA

ZFP100, a Component of the Active U7 snRNP Limiting for Histone Pre-mRNA Processing, Is Required for Entry into S Phase

Reconstitution and biochemical assays of an active human histone pre-mRNA 3'-end processing machinery

Developmental Control of Histone mRNA and dSLBP Synthesis during Drosophila Embryogenesis and the Role of dSLBP in Histone mRNA 3′ End Processing In Vivo

U7 snRNP is recruited to histone pre-mRNA in a FLASH-dependent manner by two separate regions of the stem-loop binding protein

3'-End processing of histone pre-mRNAs in Drosophila: U7 snRNP is associated with FLASH and polyadenylation factors

Histone mRNA expression: multiple levels of cell cycle regulation and important developmental consequences

U7 snRNA mutations in Drosophila block histone pre-mRNA processing and disrupt oogenesis

More than one way to make a tail

Formation of the 3′ end of histone mRNA

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