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Journal articles on the topic 'Oligomerization, ribonucleases'

Author: Grafiati
Published: 11 March 2023
Last updated: 31 July 2025

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1

Gotte, Giovanni, and Massimo Libonati. "Oligomerization of Ribonuclease A." Journal of Biological Chemistry 279, no. 35 (2004): 36670–79. http://dx.doi.org/10.1074/jbc.m404780200.

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2

Gotte, Giovanni, and Massimo Libonati. "Oligomerization of ribonuclease A under reducing conditions." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1784, no. 4 (2008): 638–50. http://dx.doi.org/10.1016/j.bbapap.2007.12.013.

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3

Libonati, M., G. Gotte, and F. Vottariello. "A Novel Biological Actions Acquired by Ribonuclease Through Oligomerization." Current Pharmaceutical Biotechnology 9, no. 3 (2008): 200–209. http://dx.doi.org/10.2174/138920108784567308.

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4

LIBONATI, Massimo, and Giovanni GOTTE. "Oligomerization of bovine ribonuclease A: structural and functional features of its multimers." Biochemical Journal 380, no. 2 (2004): 311–27. http://dx.doi.org/10.1042/bj20031922.

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Bovine pancreatic RNase A (ribonuclease A) aggregates to form various types of catalytically active oligomers during lyophilization from aqueous acetic acid solutions. Each oligomeric species is present in at least two conformational isomers. The structures of two dimers and one of the two trimers have been solved, while plausible models have been proposed for the structures of a second trimer and two tetrameric conformers. In this review, these structures, as well as the general conditions for RNase A oligomerization, based on the well known 3D (three-dimensional) domain-swapping mechanism, a
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5

Fagagnini, Andrea, Miguel Garavís, Irene Gómez-Pinto, Sabrina Fasoli, Giovanni Gotte, and Douglas V. Laurents. "NMR Characterization of Angiogenin Variants and tRNAAla Products Impacting Aberrant Protein Oligomerization." International Journal of Molecular Sciences 22, no. 3 (2021): 1439. http://dx.doi.org/10.3390/ijms22031439.

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Protein oligomerization is key to countless physiological processes, but also to abnormal amyloid conformations implicated in over 25 mortal human diseases. Human Angiogenin (h-ANG), a ribonuclease A family member, produces RNA fragments that regulate ribosome formation, the creation of new blood vessels and stress granule function. Too little h-ANG activity leads to abnormal protein oligomerization, resulting in Amyotrophic Lateral Sclerosis (ALS) or Parkinson’s disease. While a score of disease linked h-ANG mutants has been studied by X-ray diffraction, some elude crystallization. There is a
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6

Yan, Yong-Bin, Jun Zhang, Hua-Wei He, and Hai-Meng Zhou. "Oligomerization and Aggregation of Bovine Pancreatic Ribonuclease A: Characteristic Events Observed by FTIR Spectroscopy." Biophysical Journal 90, no. 7 (2006): 2525–33. http://dx.doi.org/10.1529/biophysj.105.071530.

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7

Zhang, Jun, and Yong-Bin Yan. "Oligomerization and Aggregation of Bovine Pancreatic Ribonuclease A:Backbone Hydration Probed by Infrared Band-Shift." Protein & Peptide Letters 15, no. 7 (2008): 650–57. http://dx.doi.org/10.2174/092986608785133645.

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8

Sokurenko, Yulia, Alsu Nadyrova, Vera Ulyanova, and Olga Ilinskaya. "Extracellular Ribonuclease fromBacillus licheniformis(Balifase), a New Member of the N1/T1 RNase Superfamily." BioMed Research International 2016 (2016): 1–9. http://dx.doi.org/10.1155/2016/4239375.

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The N1/T1 RNase superfamily comprises enzymes with well-established antitumor effects, such as ribotoxins secreted by fungi, primarily byAspergillusandPenicilliumspecies, and bacterial RNase secreted byB. pumilus(binase) andB. amyloliquefaciens(barnase). RNase is regarded as an alternative to classical chemotherapeutic agents due to its selective cytotoxicity towards tumor cells. New RNase with a high degree of structural similarity with binase (73%) and barnase (74%) was isolated and purified fromBacillus licheniformis(balifase, calculated molecular weight 12421.9 Da, pI 8.91). The protein sa
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9

Bombaci, Giuseppe, Mayuresh Anant Sarangdhar, Nicola Andina, et al. "LRR-protein RNH1 dampens the inflammasome activation and is associated with COVID-19 severity." Life Science Alliance 5, no. 6 (2022): e202101226. http://dx.doi.org/10.26508/lsa.202101226.

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Inflammasomes are cytosolic innate immune sensors of pathogen infection and cellular damage that induce caspase-1–mediated inflammation upon activation. Although inflammation is protective, uncontrolled excessive inflammation can cause inflammatory diseases and can be detrimental, such as in coronavirus disease (COVID-19). However, the underlying mechanisms that control inflammasome activation are incompletely understood. Here we report that the leucine-rich repeat (LRR) protein ribonuclease inhibitor (RNH1), which shares homology with LRRs of NLRP (nucleotide-binding oligomerization domain, l
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10

Canals, Albert, Joan Pous, Alı́cia Guasch, et al. "The Structure of an Engineered Domain-Swapped Ribonuclease Dimer and Its Implications for the Evolution of Proteins toward Oligomerization." Structure 9, no. 10 (2001): 967–76. http://dx.doi.org/10.1016/s0969-2126(01)00659-1.

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11

Fasoli, Sabrina, Ilaria Bettin, Riccardo Montioli, et al. "Dimerization of Human Angiogenin and of Variants Involved in Neurodegenerative Diseases." International Journal of Molecular Sciences 22, no. 18 (2021): 10068. http://dx.doi.org/10.3390/ijms221810068.

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Human Angiogenin (hANG, or ANG, 14.1 kDa) promotes vessel formation and is also called RNase 5 because it is included in the pancreatic-type ribonuclease (pt-RNase) super-family. Although low, its ribonucleolytic activity is crucial for angiogenesis in tumor tissues but also in the physiological development of the Central Nervous System (CNS) neuronal progenitors. Nevertheless, some ANG variants are involved in both neurodegenerative Parkinson disease (PD) and Amyotrophic Lateral Sclerosis (ALS). Notably, some pt-RNases acquire new biological functions upon oligomerization. Considering neurode
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12

Shankar, Kasturika, Marie N. Sorin, Himanshu Sharma, et al. "In vitro reconstitution reveals membrane clustering and RNA recruitment by the enteroviral AAA+ ATPase 2C." PLOS Pathogens 20, no. 8 (2024): e1012388. http://dx.doi.org/10.1371/journal.ppat.1012388.

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Enteroviruses are a vast genus of positive-sense RNA viruses that cause diseases ranging from common cold to poliomyelitis and viral myocarditis. They encode a membrane-bound AAA+ ATPase, 2C, that has been suggested to serve several roles in virus replication, e.g. as an RNA helicase and capsid assembly factor. Here, we report the reconstitution of full-length, poliovirus 2C’s association with membranes. We show that the N-terminal membrane-binding domain of 2C contains a conserved glycine, which is suggested by structure predictions to divides the domain into two amphipathic helix regions, wh
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13

Martins, Diogo, Bruno Salgueiro, Daniel Sobral, et al. "An endoribonuclease of the YicC-like family delays sporulation via sRNA degradation in Clostridioides difficile." Nucleic Acids Research 53, no. 13 (2025). https://doi.org/10.1093/nar/gkaf644.

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Abstract Clostridioides difficile CD25890 is a YicC-like endoribonuclease involved in regulating sporulation initiation, a process critical for the host–host transmission of this anaerobic pathogen. Using comparative transcriptomics we identified a small RNA, SQ528, that accumulates at higher levels in a CD25890 deletion mutant and we show that purified CD25890 cleaves SQ528 in a metal-dependent manner. Moreover, the overexpression of SQ528 increases sporulation under certain nutritional conditions phenocopying a CD25890 deletion mutant. CD25890 is an hexamer in solution and in vivo. An N-term
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14

Gotte, Giovanni, and Massimo Libonati. "Oligomerization of Ribonuclease A." June 25, 2004. https://doi.org/10.1074/jbc.m404780200.

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15

Tejada-Arranz, Alejandro, Aleksei Lulla, Maxime Bouilloux-Lafont, et al. "Acetylation regulates the oligomerization state and activity of RNase J, the Helicobacter pylori major ribonuclease." Nature Communications 14, no. 1 (2023). http://dx.doi.org/10.1038/s41467-023-43825-8.

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AbstractIn the gastric pathogen Helicobacter pylori, post-transcriptional regulation relies strongly on the activity of the essential ribonuclease RNase J. Here, we elucidated the crystal and cryo-EM structures of RNase J and determined that it assembles into dimers and tetramers in vitro. We found that RNase J extracted from H. pylori is acetylated on multiple lysine residues. Alanine substitution of several of these residues impacts on H. pylori morphology, and thus on RNase J function in vivo. Mutations of Lysine 649 modulates RNase J oligomerization in vitro, which in turn influences ribon
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16

Feyh, Rebecca, Nadine B. Waeber, Simone Prinz, et al. "Structure and mechanistic features of the prokaryotic minimal RNase P." eLife 10 (June 28, 2021). http://dx.doi.org/10.7554/elife.70160.

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Endonucleolytic removal of 5’-leader sequences from tRNA precursor transcripts (pre-tRNAs) by ribonuclease P (RNase P) is essential for protein synthesis. Beyond RNA-based RNase P enzymes, protein-only versions of the enzyme exert this function in various eukarya (there termed PRORPs) and in some bacteria (Aquifex aeolicus and close relatives); both enzyme types belong to distinct subgroups of the PIN domain metallonuclease superfamily. Homologs of Aquifex RNase P (HARPs) are also expressed in some other bacteria and many archaea, where they coexist with RNA-based RNase P and do not represent
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17

Cusic, Renee, and James M. Burke. "Condensation of RNase L promotes its rapid activation in response to viral infection in mammalian cells." Science Signaling 17, no. 837 (2024). http://dx.doi.org/10.1126/scisignal.adi9844.

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Oligoadenylate synthetase 3 (OAS3) and ribonuclease L (RNase L) are components of a pathway that combats viral infection in mammals. Upon detection of viral double-stranded RNA (dsRNA), OAS3 synthesizes 2′-5′-oligo(A), which activates the RNase domain of RNase L by promoting the homodimerization and oligomerization of RNase L monomers. Activated RNase L rapidly degrades all cellular mRNAs, shutting off several cellular processes. We sought to understand the molecular mechanisms underlying the rapid activation of RNase L in response to viral infection. Through superresolution microscopy and liv
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18

Sanders, Owen Davis. "Virus-Like Cytosolic and Cell-Free Oxidatively Damaged Nucleic Acids Likely Drive Inflammation, Synapse Degeneration, and Neuron Death in Alzheimer’s Disease." Journal of Alzheimer's Disease Reports, December 9, 2022, 1–19. http://dx.doi.org/10.3233/adr-220047.

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Oxidative stress, inflammation, and amyloid-β are Alzheimer’s disease (AD) hallmarks that cause each other and other AD hallmarks. Most amyloid-β-lowering, antioxidant, anti-inflammatory, and antimicrobial AD clinical trials failed; none stopped or reversed AD. Although signs suggest an infectious etiology, no pathogen accumulated consistently in AD patients. Neuropathology, neuronal cell culture, rodent, genome-wide association, epidemiological, biomarker, and clinical studies, plus analysis using Hill causality criteria and revised Koch’s postulates, indicate that the virus-like oxidative da
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