Aleksandra E Badaczewska-Dawid
Overview
Explore the profile of Aleksandra E Badaczewska-Dawid including associated specialties, affiliations and a list of published articles.
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15
Citations
145
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Recent Articles
1.
Badaczewska-Dawid A, Kolinski A
Methods Mol Biol
. 2024 Nov;
2867:55-78.
PMID: 39576575
Secondary structure elements, such as alpha helices and beta strands, play a fundamental role in defining the overall fold of a protein. Leveraging secondary structure information is essential for encoding...
2.
Badaczewska-Dawid A, Kuriata A, Pintado-Grima C, Garcia-Pardo J, Burdukiewicz M, Iglesias V, et al.
Nucleic Acids Res
. 2023 Oct;
52(D1):D360-D367.
PMID: 37897355
Protein aggregation has been associated with aging and different pathologies and represents a bottleneck in the industrial production of biotherapeutics. Numerous past studies performed in Escherichia coli and other model...
3.
Garcia-Pardo J, Badaczewska-Dawid A, Pintado-Grima C, Iglesias V, Kuriata A, Kmiecik S, et al.
Microb Cell Fact
. 2023 Sep;
22(1):186.
PMID: 37716955
Background: The budding yeast Saccharomyces cerevisiae (S. cerevisiae) is a well-established model system for studying protein aggregation due to the conservation of essential cellular structures and pathways found across eukaryotes....
4.
Badaczewska-Dawid A, Uversky V, Potoyan D
Int J Mol Sci
. 2022 Jun;
23(11).
PMID: 35682883
The liquid-liquid phase separation (LLPS) of biomolecules is a phenomenon which is nowadays recognized as the driving force for the biogenesis of numerous functional membraneless organelles and cellular bodies. The...
5.
Badaczewska-Dawid A, Nithin C, Wroblewski K, Kurcinski M, Kmiecik S
Nucleic Acids Res
. 2022 May;
50(W1):W474-W482.
PMID: 35524560
Correct identification and effective visualization of interactions in biomolecular structures facilitate understanding of their functions and molecular design. In response to the practical needs of structure-based analysis, we have created...
6.
Badaczewska-Dawid A, Garcia-Pardo J, Kuriata A, Pujols J, Ventura S, Kmiecik S
Bioinformatics
. 2022 Apr;
38(11):3121-3123.
PMID: 35445695
Summary: Protein aggregation is associated with many human disorders and constitutes a major bottleneck for producing therapeutic proteins. Our knowledge of the human protein structures repertoire has dramatically increased with...
7.
Kuriata A, Badaczewska-Dawid A, Pujols J, Ventura S, Kmiecik S
Methods Mol Biol
. 2022 Feb;
2340:17-40.
PMID: 35167068
Protein aggregation is a major hurdle in the development and manufacturing of protein-based therapeutics. Development of aggregation-resistant and stable protein variants can be guided by rational redesign using computational tools....
8.
Badaczewska-Dawid A, Kolinski A, Kmiecik S
Methods Mol Biol
. 2020 Jul;
2165:337-353.
PMID: 32621235
Conformational flexibility of protein structures can play an important role in protein function. The flexibility is often studied using computational methods since experimental characterization can be difficult. Depending on protein...
9.
Badaczewska-Dawid A, Khramushin A, Kolinski A, Schueler-Furman O, Kmiecik S
Methods Mol Biol
. 2020 Jul;
2165:273-287.
PMID: 32621231
Structural characterizations of protein-peptide complexes may require further improvements. These may include reconstruction of missing atoms and/or structure optimization leading to higher accuracy models. In this work, we describe a...
10.
Puchala W, Burdukiewicz M, Kistowski M, Dabrowska K, Badaczewska-Dawid A, Cysewski D, et al.
Bioinformatics
. 2020 Jun;
36(16):4516-4518.
PMID: 32579220
Motivation: Hydrogen-deuterium mass spectrometry (HDX-MS) is a rapidly developing technique for monitoring dynamics and interactions of proteins. The development of new devices has to be followed with new software suites...