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Items: 1 to 20 of 118


Structure of Ca2+-bound S100A4 and its interaction with peptides derived from nonmuscle myosin-IIA.

Malashkevich VN, Varney KM, Garrett SC, Wilder PT, Knight D, Charpentier TH, Ramagopal UA, Almo SC, Weber DJ, Bresnick AR.

Biochemistry. 2008 May 6;47(18):5111-26. doi: 10.1021/bi702537s. Epub 2008 Apr 15.


Structure of the S100A4/myosin-IIA complex.

Ramagopal UA, Dulyaninova NG, Varney KM, Wilder PT, Nallamsetty S, Brenowitz M, Weber DJ, Almo SC, Bresnick AR.

BMC Struct Biol. 2013 Nov 20;13:31. doi: 10.1186/1472-6807-13-31.


Crystal structure of the S100A4-nonmuscle myosin IIA tail fragment complex reveals an asymmetric target binding mechanism.

Kiss B, Duelli A, Radnai L, Kékesi KA, Katona G, Nyitray L.

Proc Natl Acad Sci U S A. 2012 Apr 17;109(16):6048-53. doi: 10.1073/pnas.1114732109. Epub 2012 Mar 28.


Two functional S100A4 monomers are necessary for regulating nonmuscle myosin-IIA and HCT116 cell invasion.

House RP, Pozzuto M, Patel P, Dulyaninova NG, Li ZH, Zencheck WD, Vitolo MI, Weber DJ, Bresnick AR.

Biochemistry. 2011 Aug 16;50(32):6920-32. doi: 10.1021/bi200498q. Epub 2011 Jul 13.


Phenothiazines inhibit S100A4 function by inducing protein oligomerization.

Malashkevich VN, Dulyaninova NG, Ramagopal UA, Liriano MA, Varney KM, Knight D, Brenowitz M, Weber DJ, Almo SC, Bresnick AR.

Proc Natl Acad Sci U S A. 2010 May 11;107(19):8605-10. doi: 10.1073/pnas.0913660107. Epub 2010 Apr 26.


Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling.

Elliott PR, Irvine AF, Jung HS, Tozawa K, Pastok MW, Picone R, Badyal SK, Basran J, Rudland PS, Barraclough R, Lian LY, Bagshaw CR, Kriajevska M, Barsukov IL.

Structure. 2012 Apr 4;20(4):654-66. doi: 10.1016/j.str.2012.02.002. Epub 2012 Apr 3.


Multilevel Changes in Protein Dynamics upon Complex Formation of the Calcium-Loaded S100A4 with a Nonmuscle Myosin IIA Tail Fragment.

Pálfy G, Kiss B, Nyitray L, Bodor A.

Chembiochem. 2016 Oct 4;17(19):1829-1838. doi: 10.1002/cbic.201600280. Epub 2016 Aug 24.


The C-terminal random coil region tunes the Ca²⁺-binding affinity of S100A4 through conformational activation.

Duelli A, Kiss B, Lundholm I, Bodor A, Petoukhov MV, Svergun DI, Nyitray L, Katona G.

PLoS One. 2014 May 15;9(5):e97654. doi: 10.1371/journal.pone.0097654. eCollection 2014.


The C-terminal region of S100A4 is important for its metastasis-inducing properties.

Zhang S, Wang G, Liu D, Bao Z, Fernig DG, Rudland PS, Barraclough R.

Oncogene. 2005 Jun 23;24(27):4401-11.


Mechanism of the Ca²+-dependent interaction between S100A4 and tail fragments of nonmuscle myosin heavy chain IIA.

Badyal SK, Basran J, Bhanji N, Kim JH, Chavda AP, Jung HS, Craig R, Elliott PR, Irvine AF, Barsukov IL, Kriajevska M, Bagshaw CR.

J Mol Biol. 2011 Jan 28;405(4):1004-26. doi: 10.1016/j.jmb.2010.11.036. Epub 2010 Nov 24.


Mts1 regulates the assembly of nonmuscle myosin-IIA.

Li ZH, Spektor A, Varlamova O, Bresnick AR.

Biochemistry. 2003 Dec 9;42(48):14258-66.


Crystal structure of metastasis-associated protein S100A4 in the active calcium-bound form.

Pathuri P, Vogeley L, Luecke H.

J Mol Biol. 2008 Oct 31;383(1):62-77. doi: 10.1016/j.jmb.2008.04.076. Epub 2008 May 7.


Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy.

Vallely KM, Rustandi RR, Ellis KC, Varlamova O, Bresnick AR, Weber DJ.

Biochemistry. 2002 Oct 22;41(42):12670-80.


Cysteine 81 is critical for the interaction of S100A4 and myosin-IIA.

Dulyaninova NG, Hite KM, Zencheck WD, Scudiero DA, Almo SC, Shoemaker RH, Bresnick AR.

Biochemistry. 2011 Aug 23;50(33):7218-27. doi: 10.1021/bi200853y. Epub 2011 Jul 21.


Regulation of myosin-IIA assembly and Mts1 binding by heavy chain phosphorylation.

Dulyaninova NG, Malashkevich VN, Almo SC, Bresnick AR.

Biochemistry. 2005 May 10;44(18):6867-76.


A biosensor of S100A4 metastasis factor activation: inhibitor screening and cellular activation dynamics.

Garrett SC, Hodgson L, Rybin A, Toutchkine A, Hahn KM, Lawrence DS, Bresnick AR.

Biochemistry. 2008 Jan 22;47(3):986-96. Epub 2007 Dec 23.


S100A4 downregulates filopodia formation through increased dynamic instability.

Goh Then Sin C, Hersch N, Rudland PS, Barraclough R, Hoffmann B, Gross SR.

Cell Adh Migr. 2011 Sep-Oct;5(5):439-47. doi: 10.4161/cam.5.5.17773.


The three-dimensional solution structure of Ca(2+)-bound S100A1 as determined by NMR spectroscopy.

Wright NT, Varney KM, Ellis KC, Markowitz J, Gitti RK, Zimmer DB, Weber DJ.

J Mol Biol. 2005 Oct 21;353(2):410-26.


S100A4 inhibits cell proliferation by interfering with the S100A1-RAGE V domain.

Khan MI, Yuan T, Chou RH, Yu C.

PLoS One. 2019 Feb 19;14(2):e0212299. doi: 10.1371/journal.pone.0212299. eCollection 2019.

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