Zobrazeno 1 - 10
of 70
pro vyhledávání: '"Alexander G Kozlov"'
Publikováno v:
eLife, Vol 4 (2015)
Escherichia coli single-stranded (ss)DNA binding (SSB) protein mediates genome maintenance processes by regulating access to ssDNA. This homotetrameric protein wraps ssDNA in multiple distinct binding modes that may be used selectively in different D
Externí odkaz:
https://doaj.org/article/b7448e1a7dea47899245e8ff58cfaa57
Publikováno v:
Nucleic Acids Research. 51:2284-2297
Escherichia coli single stranded (ss) DNA binding protein (SSB) plays essential roles in DNA maintenance. It binds ssDNA with high affinity through its N-terminal DNA binding core and recruits at least 17 different SSB interacting proteins (SIPs) tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b7183d7b5ec17c7400a80667a3ac5f01
https://doi.org/10.1093/nar/gkad084
https://doi.org/10.1093/nar/gkad084
Publikováno v:
Biophysical Journal. 122:63a-64a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::453f215dba22584a83f59bdcd86522fb
https://doi.org/10.1016/j.bpj.2022.11.551
https://doi.org/10.1016/j.bpj.2022.11.551
Publikováno v:
Nucleic Acids Research
Escherichia coli RecO is a recombination mediator protein that functions in the RecF pathway of homologous recombination, in concert with RecR, and interacts with E. coli single stranded (ss) DNA binding (SSB) protein via the last 9 amino acids of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::328182e6310cfa77793691c05418b335
https://doi.org/10.1093/nar/gkaa1291
https://doi.org/10.1093/nar/gkaa1291
Autor:
Steven J. Sandler, Antoine M. van Oijen, Nicholas E. Dixon, Lisanne M. Spenkelink, James L. Keck, Alexander G. Kozlov, Michael M. Cox, Elizabeth A. Wood, Timothy M. Lohman, Katarzyna Dubiel, Slobodan Jergic, Camille Henry
Publikováno v:
Nucleic Acids Research
Bacterial single-stranded DNA-binding proteins (SSBs) bind single-stranded DNA and help to recruit heterologous proteins to their sites of action. SSBs perform these essential functions through a modular structural architecture: the N-terminal domain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a64bca514e517b9ed299927f5f7d68b4
https://doi.org/10.1093/nar/gkaa320
https://doi.org/10.1093/nar/gkaa320
Autor:
Alexander G. Kozlov, Xian Cheng, Hongshan Zhang, Min Kyung Shinn, Elizabeth Weiland, Binh Nguyen, Irina A. Shkel, Emily Zytkiewicz, Ilya J. Finkelstein, M. Thomas Record, Timothy M. Lohman
Publikováno v:
J Mol Biol
E. coli single-stranded-DNA binding protein (EcSSB) displays nearest-neighbor (NN) and non-nearest-neighbor (NNN)) cooperativity in binding ssDNA during genome maintenance. NNN cooperativity requires the intrinsically-disordered linkers (IDL) of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b40c9a1b9101a718b847fb65bab9fb0
https://pubmed.ncbi.nlm.nih.gov/35395234
https://pubmed.ncbi.nlm.nih.gov/35395234
Autor:
Alexander G. Kozlov, Timothy M. Lohman
Publikováno v:
Biophys J
Escherichia coli single-strand (ss) DNA binding protein (SSB) is an essential protein that binds ssDNA intermediates formed during genome maintenance. SSB homotetramers bind ssDNA in two major modes, differing in occluded site size and cooperativity.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48983a627cc08efe83b86c5d0f262224
https://europepmc.org/articles/PMC8105733/
https://europepmc.org/articles/PMC8105733/
Autor:
Timothy M. Lohman, Alexander G. Kozlov
E. colisingle strand (ss) DNA binding protein (SSB) is an essential protein that binds ssDNA intermediates formed during genome maintenance. SSB homo-tetramers bind ssDNA in two major modes differing in occluded site size and cooperativity. The (SSB)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::72149aea94408cf1a31b8a7acce9f735
https://doi.org/10.1101/2020.12.05.412478
https://doi.org/10.1101/2020.12.05.412478
Autor:
Olivia L. Mooren, Timothy M. Lohman, Marlene Mekel, Patrick McConnell, John A. Cooper, Alexander G. Kozlov
Publikováno v:
Biochemistry
The heterodimeric actin capping protein (CP) is regulated by a set of proteins that contain CP-interacting (CPI) motifs. Outside of the CPI motif, the sequences of these proteins are unrelated and distinct. The CPI motif and surrounding sequences are
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6eed4994cf5297bb78d00c36171a2b7
https://pubmed.ncbi.nlm.nih.gov/32133840
https://pubmed.ncbi.nlm.nih.gov/32133840
Autor:
John A. Cooper, Marlene Mekel, Britney Johnson, Gaya K. Amarasinghe, Alexander G. Kozlov, Timothy M. Lohman, Patrick McConnell, Michael L. Gross
Publikováno v:
Cell Reports, Vol 23, Iss 9, Pp 2795-2804 (2018)
Actin assembly is important for cell motility. The ability of actin subunits to join or leave filaments via the barbed end is critical to actin dynamics. Capping protein (CP) binds to barbed ends to prevent subunit gain and loss and is regulated by p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd09ff87d37c11182ac74b446ecdc599
http://www.sciencedirect.com/science/article/pii/S2211124718306740
http://www.sciencedirect.com/science/article/pii/S2211124718306740