1987
DOI: 10.1016/s0021-9258(18)47637-5
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Properties of talin from chicken gizzard smooth muscle.

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Cited by 95 publications
(27 citation statements)
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“…The human platelet talin has been proposed to be a dumbbellshaped homodimer (Goldmann et al 1994), whereas talin purified from chicken smooth muscle appeared as a majority of flexible monomers consisting of a series of globular domains (Winkler et al 1997). The apparent molecular mass of the peptide is approximately 225 kD (Molony et al 1987;Isenberg and Goldmann 1992;Goldmann et al 1996). Talin can be cleaved by calpain II, a calcium-dependent protease also found in focal contacts, into an N-terminal and a C-terminal fragment with apparent molecular masses of 47 kD and 190-200 kD, respectively (Beckerle et al 1987;Muguruma et al 1995).…”
mentioning
confidence: 99%
“…The human platelet talin has been proposed to be a dumbbellshaped homodimer (Goldmann et al 1994), whereas talin purified from chicken smooth muscle appeared as a majority of flexible monomers consisting of a series of globular domains (Winkler et al 1997). The apparent molecular mass of the peptide is approximately 225 kD (Molony et al 1987;Isenberg and Goldmann 1992;Goldmann et al 1996). Talin can be cleaved by calpain II, a calcium-dependent protease also found in focal contacts, into an N-terminal and a C-terminal fragment with apparent molecular masses of 47 kD and 190-200 kD, respectively (Beckerle et al 1987;Muguruma et al 1995).…”
mentioning
confidence: 99%
“…Clustering many of the components into close proximity should effectively overcome their tendency to dissociate and should result in a more stable attachment. In addition, talin dimerizes at high con centrations (Molony et al 1987b), which are expected in focal adhesions. Talin dimers have not been illustrated in Figure 2 because their con formation is unknown, but they are expected to stabilize talin's association with vinculin and integrin as a result of crosslinking these components.…”
Section: Organization Of Focal Adhesionsmentioning
confidence: 95%
“…Where possible, the proteins repre sented in Figure 2 have been drawn to scale, with their morphologies based on electron microscopic images (e.g. Milam 19 85;Molony et al 1987b). In general, the location of protein binding sites has not been determined; for example, it is not known which part of the vinculin mol ecule binds to a-actinin, or vice versa.…”
Section: Organization Of Focal Adhesionsmentioning
confidence: 99%
“…Talin and radixin, found in FAs, may be similarly regulated. Talin can form dimers through self association in vitro, and electron microscopic images indicate that monomers can either fold up into a globular conformation, or appear elongated and flexible [28]. It is yet to be determined whether talin can be regulated by such conformational changes.…”
Section: Integrins and Actin Membrane Attachmentmentioning
confidence: 99%