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Structure of the active core of human stem cell factor and analysis of binding to its receptor kit.

Jiang X, Gurel O, Mendiaz EA, Stearns GW, Clogston CL, Lu HS, Osslund TD, Syed RS, Langley KE, Hendrickson WA.

EMBO J. 2000 Jul 3;19(13):3192-203.


Crystal structure of human stem cell factor: implication for stem cell factor receptor dimerization and activation.

Zhang Z, Zhang R, Joachimiak A, Schlessinger J, Kong XP.

Proc Natl Acad Sci U S A. 2000 Jul 5;97(14):7732-7.


Kit receptor dimerization is driven by bivalent binding of stem cell factor.

Lemmon MA, Pinchasi D, Zhou M, Lax I, Schlessinger J.

J Biol Chem. 1997 Mar 7;272(10):6311-7.


Structural basis for stem cell factor-KIT signaling and activation of class III receptor tyrosine kinases.

Liu H, Chen X, Focia PJ, He X.

EMBO J. 2007 Feb 7;26(3):891-901. Epub 2007 Jan 25.


Identification and characterization of a soluble c-kit receptor produced by human hematopoietic cell lines.

Turner AM, Bennett LG, Lin NL, Wypych J, Bartley TD, Hunt RW, Atkins HL, Langley KE, Parker V, Martin F, et al.

Blood. 1995 Apr 15;85(8):2052-8.


Computational simulations of stem-cell factor/c-kit receptor interaction.

Menziani MC, Fanelli F, De Benedetti PG.

Proteins. 1996 Sep;26(1):42-54.


The majority of stem cell factor exists as monomer under physiological conditions. Implications for dimerization mediating biological activity.

Hsu YR, Wu GM, Mendiaz EA, Syed R, Wypych J, Toso R, Mann MB, Boone TC, Narhi LO, Lu HS, Langley KE.

J Biol Chem. 1997 Mar 7;272(10):6406-15.


Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor.

Yuzawa S, Opatowsky Y, Zhang Z, Mandiyan V, Lax I, Schlessinger J.

Cell. 2007 Jul 27;130(2):323-34.


Soluble c-kit proteins and antireceptor monoclonal antibodies confine the binding site of the stem cell factor.

Blechman JM, Lev S, Brizzi MF, Leitner O, Pegoraro L, Givol D, Yarden Y.

J Biol Chem. 1993 Feb 25;268(6):4399-406.


Human stem cell factor dimer forms a complex with two molecules of the extracellular domain of its receptor, Kit.

Philo JS, Wen J, Wypych J, Schwartz MG, Mendiaz EA, Langley KE.

J Biol Chem. 1996 Mar 22;271(12):6895-902.


Changes in conformation and stability upon SCF/sKit complex formation.

Narhi LO, Wypych J, Li T, Langley KE, Arakawa T.

J Protein Chem. 1998 Jul;17(5):387-96.


Analysis of c-kit receptor dimerization by fluorescence resonance energy transfer.

Broudy VC, Lin NL, B├╝hring HJ, Komatsu N, Kavanagh TJ.

Blood. 1998 Feb 1;91(3):898-906.


Activation of the human c-kit product by ligand-induced dimerization mediates circular actin reorganization and chemotaxis.

Blume-Jensen P, Claesson-Welsh L, Siegbahn A, Zsebo KM, Westermark B, Heldin CH.

EMBO J. 1991 Dec;10(13):4121-8.


Flt3 ligand structure and unexpected commonalities of helical bundles and cystine knots.

Savvides SN, Boone T, Andrew Karplus P.

Nat Struct Biol. 2000 Jun;7(6):486-91.


Structure-function analyses of the kit receptor for the steel factor.

Blechman JM, Lev S, Givol D, Yarden Y.

Stem Cells. 1993 Jul;11 Suppl 2:12-21. Review.


Stem cell factor and c-kit are expressed by and may affect vascular SMCs through an autocrine pathway.

Hollenbeck ST, Sakakibara K, Faries PL, Workhu B, Liu B, Kent KC.

J Surg Res. 2004 Aug;120(2):288-94.

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