🔬 A new study by EMBL researchers, published in @science.org, about the pre-ribosome assembly pathways inside intact human cells, reveals — at molecular resolution — in-cell structural snapshots of both ribosomal subunit precursors, the SSU processome and the pre-60S, and novel configurations.
September 25, 2026 at 8:43 AM
🔬 A new study by EMBL researchers, published in @science.org, about the pre-ribosome assembly pathways inside intact human cells, reveals — at molecular resolution — in-cell structural snapshots of both ribosomal subunit precursors, the SSU processome and the pre-60S, and novel configurations.
Nature research paper: Helicase-mediated mechanism of SSU processome maturation and disassembly
go.nature.com/47hsA99
go.nature.com/47hsA99
Helicase-mediated mechanism of SSU processome maturation and disassembly - Nature
Structural studies of 16 native yeast ribosomal small subunit processome structures provide insights into the mechanisms governing the transformation into a pre-40S particle.
go.nature.com
October 31, 2025 at 3:34 PM
Nature research paper: Helicase-mediated mechanism of SSU processome maturation and disassembly
go.nature.com/47hsA99
go.nature.com/47hsA99
This is an astounding paper, but hard to read if you're not an expert. The news release I linked above tells the story better than I could. Here's the paper. It's just ... wow!
This work will be admired 100 years from now ... If there are still scientists then 😞.
www.nature.com/articles/s41...
This work will be admired 100 years from now ... If there are still scientists then 😞.
www.nature.com/articles/s41...
Helicase-mediated mechanism of SSU processome maturation and disassembly - Nature
Structural studies of 16 native yeast ribosomal small subunit processome structures provide insights into the mechanisms governing the transformation into a pre-40S particle.
www.nature.com
October 31, 2025 at 2:39 AM
This is an astounding paper, but hard to read if you're not an expert. The news release I linked above tells the story better than I could. Here's the paper. It's just ... wow!
This work will be admired 100 years from now ... If there are still scientists then 😞.
www.nature.com/articles/s41...
This work will be admired 100 years from now ... If there are still scientists then 😞.
www.nature.com/articles/s41...
Helicase-mediated mechanism of SSU processome maturation and disassembly https://www.biorxiv.org/content/10.1101/2025.09.29.679232v1
September 30, 2025 at 4:46 AM
Helicase-mediated mechanism of SSU processome maturation and disassembly https://www.biorxiv.org/content/10.1101/2025.09.29.679232v1
RRIDs were included in this paper. We value the author's support of reproducibility. #ReproducibleResearch #OpenScience #accelerateopenscience
Helicase-mediated mechanism of SSU processome maturation and disassembly
doi.org
December 21, 2025 at 8:00 AM
RRIDs were included in this paper. We value the author's support of reproducibility. #ReproducibleResearch #OpenScience #accelerateopenscience
U Three Protein 18 small subunit processome component (UTP18:p) is a component of the nucleolar small subunit processome for some, as of yet unknown, purpose. Its brightly lit S+phosphoryl acceptors are adjacent to low complexity D/E regions that appear to bracket an unnamed ~50 aa helical domain.
February 16, 2025 at 1:39 PM
U Three Protein 18 small subunit processome component (UTP18:p) is a component of the nucleolar small subunit processome for some, as of yet unknown, purpose. Its brightly lit S+phosphoryl acceptors are adjacent to low complexity D/E regions that appear to bracket an unnamed ~50 aa helical domain.
RRIDs were included in this paper. We value the author's support of reproducibility. #OpenScience #accelerateopenscience #ReproducibleResearch
Helicase-mediated mechanism of SSU processome maturation and disassembly
doi.org
October 8, 2025 at 7:00 AM
RRIDs were included in this paper. We value the author's support of reproducibility. #OpenScience #accelerateopenscience #ReproducibleResearch
U Three Protein 18 small subunit processome component (UTP18:p) is a component of the nucleolar small subunit processome for some, as of yet unknown, purpose. Its brightly lit S+phosphoryl acceptors are adjacent to low complexity D/E regions that appear to bracket an unnamed ~50 aa helical domain.
February 16, 2025 at 1:25 PM
U Three Protein 18 small subunit processome component (UTP18:p) is a component of the nucleolar small subunit processome for some, as of yet unknown, purpose. Its brightly lit S+phosphoryl acceptors are adjacent to low complexity D/E regions that appear to bracket an unnamed ~50 aa helical domain.
Tryptophan aspartic acid repeat containing protein 46 (WDR46:p) is found in the nucleolus, where it is believed to be part of the small ribosomal subunit (SSU) processome. It has one of the classic phosphoIDR patterns, with one (or more) major, lit acceptors in an N-terminal IDR. #proteomics
February 15, 2025 at 12:37 PM
Tryptophan aspartic acid repeat containing protein 46 (WDR46:p) is found in the nucleolus, where it is believed to be part of the small ribosomal subunit (SSU) processome. It has one of the classic phosphoIDR patterns, with one (or more) major, lit acceptors in an N-terminal IDR. #proteomics
Tryptophan aspartic acid repeat containing protein 3 (WDR3:p) is believed to be part of the nucleolar small subunit processome. The human version has enhanced phosphorylation at the lit nward SP+phosphoryl acceptor, most likely associated with nucleolar cell cycle fan dance. #proteomics
February 14, 2025 at 1:19 PM
Tryptophan aspartic acid repeat containing protein 3 (WDR3:p) is believed to be part of the nucleolar small subunit processome. The human version has enhanced phosphorylation at the lit nward SP+phosphoryl acceptor, most likely associated with nucleolar cell cycle fan dance. #proteomics
Periodic tryptophan protein 2 homolog small subunit processome component [?] (PWP2:p) is found in the nucleolus with 2 prominent WD40-type β-propellers (yes, W & D are the amino acids, too). All 3 of the cward S+phosphoryl acceptors are normally lit. #proteomics
February 13, 2025 at 1:20 PM
Periodic tryptophan protein 2 homolog small subunit processome component [?] (PWP2:p) is found in the nucleolus with 2 prominent WD40-type β-propellers (yes, W & D are the amino acids, too). All 3 of the cward S+phosphoryl acceptors are normally lit. #proteomics
Tryptophan aspartic acid repeat containing protein 46 (WDR46:p) is found in the nucleolus, where it is believed to be part of the small ribosomal subunit (SSU) processome. It has one of the classic phosphoIDR patterns, with one (or more) major, lit acceptors in an N-terminal IDR. #proteomics
February 15, 2025 at 12:37 PM
Tryptophan aspartic acid repeat containing protein 46 (WDR46:p) is found in the nucleolus, where it is believed to be part of the small ribosomal subunit (SSU) processome. It has one of the classic phosphoIDR patterns, with one (or more) major, lit acceptors in an N-terminal IDR. #proteomics
Tryptophan aspartic acid repeat containing protein 3 (WDR3:p) is believed to be part of the nucleolar small subunit processome. The human version has enhanced phosphorylation at the lit nward SP+phosphoryl acceptor, most likely associated with nucleolar cell cycle fan dance. #proteomics
February 14, 2025 at 1:25 PM
Tryptophan aspartic acid repeat containing protein 3 (WDR3:p) is believed to be part of the nucleolar small subunit processome. The human version has enhanced phosphorylation at the lit nward SP+phosphoryl acceptor, most likely associated with nucleolar cell cycle fan dance. #proteomics
Periodic tryptophan protein 2 homolog small subunit processome component ?] (PWP2:p) is found in the nucleolus with 2 prominent WD40-type β-propellers (yes, W & D are the amino acids, too). All 3 of the cward S+phosphoryl acceptors are normally lit. [<a href="/hashtag/proteomics" class="hover:underline text-blue-600 dark:text-sky-400 no-card-link">#proteomics
February 13, 2025 at 1:22 PM
Periodic tryptophan protein 2 homolog small subunit processome component ?] (PWP2:p) is found in the nucleolus with 2 prominent WD40-type β-propellers (yes, W & D are the amino acids, too). All 3 of the cward S+phosphoryl acceptors are normally lit. [<a href="/hashtag/proteomics" class="hover:underline text-blue-600 dark:text-sky-400 no-card-link">#proteomics
Helicase-mediated mechanism of SSU processome maturation and disassembly https://www.biorxiv.org/content/10.1101/2025.09.29.679232v1
September 30, 2025 at 4:46 AM
Helicase-mediated mechanism of SSU processome maturation and disassembly https://www.biorxiv.org/content/10.1101/2025.09.29.679232v1
[Nature.com]Helicase-mediated mechanism of SSU processome maturation and disassembly - Nature Structural studies of 16 native yeast ribosomal small subunit processome structures provide insights into the mechanisms governing the transformation into a pre-40S particle.
November 1, 2025 at 6:45 PM
[Nature.com]Helicase-mediated mechanism of SSU processome maturation and disassembly - Nature Structural studies of 16 native yeast ribosomal small subunit processome structures provide insights into the mechanisms governing the transformation into a pre-40S particle.
Helicase-mediated mechanism of SSU processome maturation and disassembly
Helicase-mediated mechanism of SSU processome maturation and disassembly
Nature, Published online: 29 October 2025; doi:10.1038/s41586-025-09688-3 Structural studies of 16 native yeast ribosomal small subunit processome structures provide insights into the mechanisms governing the transformation into a pre-40S particle.
www.nature.com
October 29, 2025 at 5:28 PM
Helicase-mediated mechanism of SSU processome maturation and disassembly