Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Diane Ternent"'
Publikováno v:
Molecular microbiology. 22(3)
Salmonella enterica serovar blegdam has a restriction and modification system encoded by genes linked to serB. We have cloned these genes, putative alleles of the hsd locus of Escherichia coli K-12, and confirmed by the sequence similarities of flank
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d93028f37acb601504ab9fbded5007ca
https://pubmed.ncbi.nlm.nih.gov/28777503
https://pubmed.ncbi.nlm.nih.gov/28777503
Autor:
Celine Renoult, Yves Benyamin, Claude Roustan, Abdellatif Fattoum, Fabrice Raynaud, Laurence Blondin, Sutherland K. Maciver, Diane Ternent
Publikováno v:
European Journal of Biochemistry. 268:6165-6175
It is generally assumed that of the six domains that comprise gelsolin, domain 2 is primarily responsible for the initial contact with the actin filament that will ultimately result in the filament being severed. Other actin-binding regions within do
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf7f6b255c730f9c366b5e86d4ff5590
https://doi.org/10.1046/j.0014-2956.2001.02574.x
https://doi.org/10.1046/j.0014-2956.2001.02574.x
Publikováno v:
European Journal of Biochemistry. 267:3378-3384
Cofilin is a small actin-binding protein that is known to bind both F-actin and G-actin, severing the former. The interaction of cofilin with actin is pH-sensitive, F-actin being preferentially bound at low pH and G-actin at higher pH, within the phy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2d89e8656a380649a577f47f9b39d27e
https://doi.org/10.1046/j.1432-1327.2000.01372.x
https://doi.org/10.1046/j.1432-1327.2000.01372.x
The specificity of StySKI, a type I restriction enzyme, implies a structure with rotational symmetry
Publikováno v:
Nucleic Acids Research. 25:1694-1700
The type I restriction and modification (R-M) enzyme from Salmonella enterica serovar kaduna ( Sty SKI) recognises the DNA sequence 5'-CGAT(N)7GTTA, an unusual target for a type I R-M system in that it comprises two tetranucleotide components. The am
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6f78c88d67f1515495ab2675b3ac2a0
https://doi.org/10.1093/nar/25.9.1694
https://doi.org/10.1093/nar/25.9.1694
Publikováno v:
The EMBO Journal. 15:2003-2009
One subunit of both type I and type III restriction and modification enzymes contains motifs characteristic of DEAD box proteins, which implies that these enzymes may be DNA helicases. This subunit is essential for restriction, but not modification.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::632755e2faf10d58854abcacbc0ec502
https://doi.org/10.1002/j.1460-2075.1996.tb00551.x
https://doi.org/10.1002/j.1460-2075.1996.tb00551.x
Autor:
Emeline Lagarrigue, Sutherland K. Maciver, Claude Roustan, Yves Benyamin, Abdellatif Fattoum, Diane Ternent
Publikováno v:
European journal of biochemistry. 270(20)
Gelsolin is a multidomain and multifunction protein that nucleates the assembly of filaments and severs them. The activation of gelsolin by calcium is a multistep process involving many calcium binding sites that act to unfold the molecule from a tig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44eb4c56bef5f164816a21b40b658341
https://pubmed.ncbi.nlm.nih.gov/14519122
https://pubmed.ncbi.nlm.nih.gov/14519122
Autor:
Sutherland K. Maciver, Celine Renoult, Catherine Astier, Yves Benyamin, Claude Roustan, Diane Ternent, Abdellatif Fattoum
Publikováno v:
The Journal of biological chemistry. 274(41)
The cofilins are members of a protein family that binds monomeric and filamentous actin, severs actin filaments, and increases monomer off-rate from the pointed end. Here, we characterize the cofilin-actin interface. We confirm earlier work suggestin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbe8cdb710e87d4d02294442a54a8a29
https://pubmed.ncbi.nlm.nih.gov/10506133
https://pubmed.ncbi.nlm.nih.gov/10506133
Publikováno v:
Molecular Microbiology. 23:851-851
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8b0187be19d1da18fdf96cb35eeaed1d
https://doi.org/10.1111/j.1551-2916.2005.00526.x-i1
https://doi.org/10.1111/j.1551-2916.2005.00526.x-i1
Publikováno v:
FEBS Letters. (1):71-75
Gelsolin is an actin filament severing protein composed of six similar structured domains that differ with respect to actin, calcium and polyphospho-inositide binding. Previous work has established that gelsolin binds tropomyosin [Koepf, E.K. and Bur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0aee4156f9d9fdab15fc3ac2a84aac13