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Table representation of search results timeline featuring number of search results per year.
Year | Number of Results |
---|---|
1991 | 1 |
1998 | 1 |
1999 | 1 |
2000 | 1 |
2001 | 1 |
2002 | 1 |
2024 | 0 |
PubMed for id: 128735
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Vinexin, CAP/ponsin, ArgBP2: a novel adaptor protein family regulating cytoskeletal organization and signal transduction.
Cell Struct Funct. 2002 Feb;27(1):1-7. doi: 10.1247/csf.27.1.
Cell Struct Funct. 2002.
PMID: 11937713
Free article.
Review.
The sorbin homology domain: a motif for the targeting of proteins to lipid rafts.
Kimura A, Baumann CA, Chiang SH, Saltiel AR.
Kimura A, et al.
Proc Natl Acad Sci U S A. 2001 Jul 31;98(16):9098-103. doi: 10.1073/pnas.151252898.
Proc Natl Acad Sci U S A. 2001.
PMID: 11481476
Free PMC article.
Item in Clipboard
Inhibitory effect of sorbin on pepsin secretion in conscious cats and rabbits.
Charpin-Elhamri G, Elbaba M, Descroix-Vagne M, Pansu D, Perret JP.
Charpin-Elhamri G, et al.
Peptides. 2000 Jan;21(1):65-72. doi: 10.1016/s0196-9781(99)00175-8.
Peptides. 2000.
PMID: 10704721
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nArgBP2, a novel neural member of ponsin/ArgBP2/vinexin family that interacts with synapse-associated protein 90/postsynaptic density-95-associated protein (SAPAP).
Kawabe H, Hata Y, Takeuchi M, Ide N, Mizoguchi A, Takai Y.
Kawabe H, et al.
J Biol Chem. 1999 Oct 22;274(43):30914-8. doi: 10.1074/jbc.274.43.30914.
J Biol Chem. 1999.
PMID: 10521485
Free article.
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A role for CAP, a novel, multifunctional Src homology 3 domain-containing protein in formation of actin stress fibers and focal adhesions.
Ribon V, Herrera R, Kay BK, Saltiel AR.
Ribon V, et al.
J Biol Chem. 1998 Feb 13;273(7):4073-80. doi: 10.1074/jbc.273.7.4073.
J Biol Chem. 1998.
PMID: 9461600
Free article.
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Isolation and characterisation of porcine sorbin.
Vagne-Descroix M, Pansu D, Jörnvall H, Carlquist M, Guignard H, Jourdan G, Desvigne A, Collinet M, Caillet C, Mutt V.
Vagne-Descroix M, et al.
Eur J Biochem. 1991 Oct 1;201(1):53-9. doi: 10.1111/j.1432-1033.1991.tb16254.x.
Eur J Biochem. 1991.
PMID: 1915377
Free article.
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