Relevant bibliographies by topics / Oligomerization, ribonucleases

Contents

  1. Journal articles
  2. Dissertations / Theses

Academic literature on the topic 'Oligomerization, ribonucleases'

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

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Oligomerization, ribonucleases.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Oligomerization, ribonucleases"

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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Oligomerization, ribonucleases"

1

Nissbeck, Mikael. "Determining the oligomeric structure of PARN." Thesis, Uppsala universitet, Institutionen för cell- och molekylärbiologi, 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-167233.

Full text
Abstract:
Poly(A)-specific ribonuclease (PARN) is a deadenylase that degrades the poly(A) tail of eukaryotic mRNA. PARN also interacts with the 5’-cap structure of the mRNA. The binding of the cap structure enhances the deadenylation rate. PARN has previously been described as a dimer. We have studied PARN with size exclusion chromatography to investigate the oligomeric composition and revealed oligomeric compositions of PARN that are larger than dimeric PARN. Deadenylation assays have been used to measure the cap stimulated activity of PARN. The deadenylation assays showed that the cap stimulated activ
APA, Harvard, Vancouver, ISO, and other styles
2

sabrina, fasoli. "STRUCTURAL DETERMINANTS AFFECTING THE OLIGOMERIZATION TENDENCY OF SOME PANCREATIC RIBONUCLEASES." Doctoral thesis, 2020. http://hdl.handle.net/11562/1017109.

Full text
Abstract:
The three dimensional domain swapping (3D-DS) mechanism represents a useful strategy that proteins can follow to self-associate. This mechanism requires the presence of a flexible portion that generally links the N- and/or C-terminus of the protein to its core. This portion, called hinge loop, can adopt different conformations as a function of the environmental conditions and allows the mentioned N- and/or C-terminal domains to be detached from the protein core and to be swapped with an identical domain of another protomer. This induces the formation of dimer(s) or larger oligomer(s) that ofte
APA, Harvard, Vancouver, ISO, and other styles
3

FAGAGNINI, ANDREA. "Oligomerization of RNase A and onconase: structural determinants and influence on the functional features of the two enzymes." Doctoral thesis, 2017. http://hdl.handle.net/11562/961013.

Full text
Abstract:
In the work I report and analyze the strong influence of RNase A deamidation on the enzyme tendency to oligomerize, the structural and functional differences induced by three oligomerization methods on RNase A monomer and dimers, and the structural features of a dimeric species produced by induced ONC oligomerization
APA, Harvard, Vancouver, ISO, and other styles
4

VOTTARIELLO, FRANCESCA. "OLIGOMERIZATION OF RNase A:a) A STUDY OF THE INFLUENCE OF SERINE 80 RESIDUE ON THE 3D DOMAIN SWAPPING MECHANISMb) “ZERO-LENGTH” DIMERS OF RNase A AND THEIR CATIONIZATION WITH PEI." Doctoral thesis, 2010. http://hdl.handle.net/11562/344075.

Full text
Abstract:
"Zero-length" dimers of ribonuclease A, a novel type of dimers formed by two RNase A molecules bound to each other through a zero-length amide bond [Simons, B.L. et al. (2007) Proteins 66, 183-195], were analyzed, and tested for their possible in vitro cytotoxic activity. Results: (i) Besides dimers, also trimers and higher oligomers can be identified among the products of the covalently linking reaction. (ii) The "zero-length" dimers prepared by us appear not to be a unique species, as was instead reported by Simons et al. The product is heterogeneous, as shown by the involvement in the amide
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Oligomerization, ribonucleases' for particular source types:
Journal articles
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography