2010
DOI: 10.1074/jbc.m109.095109
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Influence of Heparin Mimetics on Assembly of the FGF·FGFR4 Signaling Complex

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Cited by 31 publications
(36 citation statements)
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“…According to the calculated H-bonding frequencies (Fig. 5a), Asn 18, Lys 112, Lys 113, Arg 122 and Arg 128 form the most frequently observed H-bonds with IdoA2S units of HE dp6, highlighting the particular importance of IdoA2S sulfate groups in binding, which is in good agreement with previous SPR measurements [50]. Similarly, from the MD simulations of these three FGF1-HE crystal structures, only the central GlcNS was comparable to IdoA2S units in terms of H-bonding frequencies.…”
Section: Resultssupporting
confidence: 89%
“…According to the calculated H-bonding frequencies (Fig. 5a), Asn 18, Lys 112, Lys 113, Arg 122 and Arg 128 form the most frequently observed H-bonds with IdoA2S units of HE dp6, highlighting the particular importance of IdoA2S sulfate groups in binding, which is in good agreement with previous SPR measurements [50]. Similarly, from the MD simulations of these three FGF1-HE crystal structures, only the central GlcNS was comparable to IdoA2S units in terms of H-bonding frequencies.…”
Section: Resultssupporting
confidence: 89%
“…B, DP required for complex formation between FGF2 and polySia. Left panel, FGF2 (100 ng) was incubated without (none) or with oligo/polySia (DP ϭ 1-10 (mixture of 1-10), DP ϭ 11-20 (mixture of [11][12][13][14][15][16][17][18][19][20], DP ϭ 21-30 (mixture of [21][22][23][24][25][26][27][28][29][30], and DP ϭ 31-40 (mixture of [21][22][23][24][25][26][27][28][29][30]) in TBS at 37°C for 2 h. Right upper panel, FGF2 (100 ng) was incubated with polySia with defined DP (DP ϭ 11-16) in TBS at 37°C for 2 h. Right lower panel, FGF2 (100 ng) was incubated with polySia with defined DP (DP ϭ 15-24) in TBS at 37°C for 2 h. Samples were analyzed by horizontal native-PAGE. Arrowhead, origin; Ϫ, cathode; ϩ, anode.…”
Section: Resultsmentioning
confidence: 99%
“…FGF2 exhibits high affinity to IIIc-type FGFR-1 and -2 and low affinity to IIIctype FGFR-3 (27,28). FGF2 is also known to have affinity to heparan sulfate (HS) proteoglycan (19), with the HS of HS proteoglycan functioning as the key molecule for the formation of the ternary complex with FGF2 and FGFR (29,30). The K d values of FGF2 binding to HS and FGFR-1 are 39 and 62 nM, respectively, as determined by the surface plasmon resonance (SPR) (31) method.…”
mentioning
confidence: 99%
“…Lipid/membrane interactions Polysaccharide interactions Protein/peptide interactions with polymers and nanoparticles …”
Section: Introductionmentioning
confidence: 99%