Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Mikita Misiura"'
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 90:1278-1290
Prediction of side chain conformations of amino acids in proteins (also termed ‘packing’) is an important and challenging part of protein structure prediction with many interesting applications in protein design. A variety of methods for packing
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cff2057b422a2566701d2c4608dcd28a
https://doi.org/10.1002/prot.26311
https://doi.org/10.1002/prot.26311
Autor:
Carson C. Cole, Mikita Misiura, Sarah A. H. Hulgan, Caroline M. Peterson, Joseph W. Williams, Anatoly B. Kolomeisky, Jeffrey D. Hartgerink
Publikováno v:
Biomacromolecules. 23(11)
Cation-π interactions play a significant role in the stabilization of globular proteins. However, their role in collagen triple helices is less well understood and they have rarely been used in de novo designed collagen mimetic systems. In this stud
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2fe348dbede3be735213dd31e08d700e
https://pubmed.ncbi.nlm.nih.gov/36239387
https://pubmed.ncbi.nlm.nih.gov/36239387
Autor:
Mikita Misiura, Anatoly B. Kolomeisky
Publikováno v:
The journal of physical chemistry. B. 124(1)
Although intrinsically disordered proteins and intrinsically disordered regions (IDRs) in folded proteins are not able to form stable structures, it is known that they play critically important roles in various biological processes. However, despite
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d691ca5987aca85922676aed2fa6213
https://pubmed.ncbi.nlm.nih.gov/31804089
https://pubmed.ncbi.nlm.nih.gov/31804089
Publikováno v:
J Chem Phys
Trapping by active sites on surfaces plays important roles in various chemical and biological processes, including catalysis, enzymatic reactions, and viral entry into host cells. However, the mechanisms of these processes remain not well understood,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d42880e0fb84bb81410b87c700910bb
https://doi.org/10.1063/5.0069917
https://doi.org/10.1063/5.0069917
Autor:
Anatoly B. Kolomeisky, Mikita Misiura
Publikováno v:
The Journal of chemical physics. 150(15)
ERK2 is a kinase protein that belongs to a Ras/Raf/MEK/ERK signaling pathway, which is activated in response to a range of extracellular signals. Malfunctioning of this cascade leads to a variety of serious diseases, including cancers. This is often
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f227a0669465be79dc940506cdeee89
https://pubmed.ncbi.nlm.nih.gov/31005085
https://pubmed.ncbi.nlm.nih.gov/31005085
Autor:
Anatoly B. Kolomeisky, Mikita Misiura
ERK2 is a kinase protein that belongs to a Ras/Raf/MEK/ERK signalling pathway, which is activated in response to a range of extracellular signals. Malfunctioning of this cascade leads to variety of serious diseases, including cancers. This is often c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4712f563d3288ac1c3dfcae23e7c6d7
https://doi.org/10.1101/409482
https://doi.org/10.1101/409482
Publikováno v:
The journal of physical chemistry. B. 122(29)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c90d294906538ade11e82ce380cd630
https://pubmed.ncbi.nlm.nih.gov/29630822
https://pubmed.ncbi.nlm.nih.gov/29630822
Publikováno v:
The journal of physical chemistry. B. 122(17)
Motor proteins are active enzymatic molecules that are critically important for a variety of biological phenomena. It is known that some neurodegenerative diseases are caused by specific mutations in motor proteins that lead to their malfunctioning.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a601483784b6ea5f82d0e572545c0c9
https://pubmed.ncbi.nlm.nih.gov/29995413
https://pubmed.ncbi.nlm.nih.gov/29995413
Autor:
Anatoly B. Kolomeisky, Mikita Misiura
Publikováno v:
Biophysical Journal. 116:198a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::30972a6a2193b481690901a8ded77fa5
https://doi.org/10.1016/j.bpj.2018.11.1097
https://doi.org/10.1016/j.bpj.2018.11.1097
Autor:
Anatoly B. Kolomeisky, Mikita Misiura
Publikováno v:
The journal of physical chemistry. B. 120(40)
ERK2 are protein kinases that during the enzymatic catalysis, in contrast to traditional enzymes, utilize additional interactions with substrates outside of the active sites. It is widely believed that these docking interactions outside of the enzyma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78a13531293f7c19878759dd33808975
https://pubmed.ncbi.nlm.nih.gov/27649451
https://pubmed.ncbi.nlm.nih.gov/27649451