Format
Sort by

Send to

Choose Destination

Links from PubMed

Items: 1 to 20 of 107

1.

Structures of lysenin reveal a shared evolutionary origin for pore-forming proteins and its mode of sphingomyelin recognition.

De Colibus L, Sonnen AF, Morris KJ, Siebert CA, Abrusci P, Plitzko J, Hodnik V, Leippe M, Volpi E, Anderluh G, Gilbert RJ.

Structure. 2012 Sep 5;20(9):1498-507. doi: 10.1016/j.str.2012.06.011. Epub 2012 Jul 19.

2.

The single-giant unilamellar vesicle method reveals lysenin-induced pore formation in lipid membranes containing sphingomyelin.

Alam JM, Kobayashi T, Yamazaki M.

Biochemistry. 2012 Jun 26;51(25):5160-72. doi: 10.1021/bi300448g. Epub 2012 Jun 15.

PMID:
22668506
3.

Cholesterol and lipid/protein ratio control the oligomerization of a sphingomyelin-specific toxin, lysenin.

Ishitsuka R, Kobayashi T.

Biochemistry. 2007 Feb 13;46(6):1495-502. Epub 2007 Jan 23.

PMID:
17243772
4.

Visualization of Lipid Membrane Reorganization Induced by a Pore-Forming Toxin Using High-Speed Atomic Force Microscopy.

Yilmaz N, Kobayashi T.

ACS Nano. 2015 Aug 25;9(8):7960-7. doi: 10.1021/acsnano.5b01041. Epub 2015 Aug 6.

PMID:
26222645
5.

Biology of lysenin, a protein in the coelomic fluid of the earthworm Eisenia foetida.

Kobayashi H, Ohta N, Umeda M.

Int Rev Cytol. 2004;236:45-99. Review.

PMID:
15261736
6.

Secondary structure and orientation of the pore-forming toxin lysenin in a sphingomyelin-containing membrane.

Hereć M, Gagoś M, Kulma M, Kwiatkowska K, Sobota A, Gruszecki WI.

Biochim Biophys Acta. 2008 Apr;1778(4):872-9. doi: 10.1016/j.bbamem.2007.12.004. Epub 2007 Dec 15.

7.

Oligomerization and pore formation of a sphingomyelin-specific toxin, lysenin.

Yamaji-Hasegawa A, Makino A, Baba T, Senoh Y, Kimura-Suda H, Sato SB, Terada N, Ohno S, Kiyokawa E, Umeda M, Kobayashi T.

J Biol Chem. 2003 Jun 20;278(25):22762-70. Epub 2003 Apr 3.

8.

Recognition of sphingomyelin by lysenin and lysenin-related proteins.

Kiyokawa E, Makino A, Ishii K, Otsuka N, Yamaji-Hasegawa A, Kobayashi T.

Biochemistry. 2004 Aug 3;43(30):9766-73.

PMID:
15274631
9.

Sphingomyelin-rich domains are sites of lysenin oligomerization: implications for raft studies.

Kulma M, Hereć M, Grudziński W, Anderluh G, Gruszecki WI, Kwiatkowska K, Sobota A.

Biochim Biophys Acta. 2010 Mar;1798(3):471-81. doi: 10.1016/j.bbamem.2009.12.004. Epub 2009 Dec 16.

10.

Molecular mechanism of sphingomyelin-specific membrane binding and pore formation by actinoporins.

Bakrac B, Anderluh G.

Adv Exp Med Biol. 2010;677:106-15. Review.

PMID:
20687484
11.

Lysenin-His, a sphingomyelin-recognizing toxin, requires tryptophan 20 for cation-selective channel assembly but not for membrane binding.

Kwiatkowska K, Hordejuk R, Szymczyk P, Kulma M, Abdel-Shakor AB, Płucienniczak A, Dołowy K, Szewczyk A, Sobota A.

Mol Membr Biol. 2007 Mar-Apr;24(2):121-34.

PMID:
17453419
12.

Earthworm-derived pore-forming toxin lysenin and screening of its inhibitors.

Sukumwang N, Umezawa K.

Toxins (Basel). 2013 Aug 8;5(8):1392-401. doi: 10.3390/toxins5081392. Review.

13.

Real-time visualization of assembling of a sphingomyelin-specific toxin on planar lipid membranes.

Yilmaz N, Yamada T, Greimel P, Uchihashi T, Ando T, Kobayashi T.

Biophys J. 2013 Sep 17;105(6):1397-405. doi: 10.1016/j.bpj.2013.07.052.

14.

Lysenin, a unique sphingomyelin-binding protein.

Shakor AB, Czurylo EA, Sobota A.

FEBS Lett. 2003 May 8;542(1-3):1-6. Review.

15.

Dissection of the mechanisms of cytolytic and antibacterial activity of lysenin, a defence protein of the annelid Eisenia fetida.

Bruhn H, Winkelmann J, Andersen C, Andrä J, Leippe M.

Dev Comp Immunol. 2006;30(7):597-606. Epub 2005 Oct 5.

PMID:
16386304
16.

Lysenin, a novel sphingomyelin-specific binding protein.

Yamaji A, Sekizawa Y, Emoto K, Sakuraba H, Inoue K, Kobayashi H, Umeda M.

J Biol Chem. 1998 Feb 27;273(9):5300-6.

17.

Lysenin: a sphingomyelin specific pore-forming toxin.

Shogomori H, Kobayashi T.

Biochim Biophys Acta. 2008 Mar;1780(3):612-8. Epub 2007 Sep 15. Review.

PMID:
17980968
18.

Membrane cholesterol and sphingomyelin, and ostreolysin A are obligatory for pore-formation by a MACPF/CDC-like pore-forming protein, pleurotolysin B.

Ota K, Leonardi A, Mikelj M, Skočaj M, Wohlschlager T, Künzler M, Aebi M, Narat M, Križaj I, Anderluh G, Sepčić K, Maček P.

Biochimie. 2013 Oct;95(10):1855-64. doi: 10.1016/j.biochi.2013.06.012. Epub 2013 Jun 25.

PMID:
23806422
19.

Nanomechanical recognition of sphingomyelin-rich membrane domains by atomic force microscopy.

Wang T, Shogomori H, Hara M, Yamada T, Kobayashi T.

Biochemistry. 2012 Jan 10;51(1):74-82. doi: 10.1021/bi2011652. Epub 2011 Dec 15.

PMID:
22148674
20.

2NH and 3OH are crucial structural requirements in sphingomyelin for sticholysin II binding and pore formation in bilayer membranes.

Maula T, Isaksson YJ, García-Linares S, Niinivehmas S, Pentikäinen OT, Kurita M, Yamaguchi S, Yamamoto T, Katsumura S, Gavilanes JG, Martínez-del-Pozo A, Slotte JP.

Biochim Biophys Acta. 2013 May;1828(5):1390-5. doi: 10.1016/j.bbamem.2013.01.018. Epub 2013 Jan 30.

Items per page

Supplemental Content

Write to the Help Desk