ライフサイエンスコーパス: tenascin-R

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1 extracellular matrix proteins tenascin-C and tenascin-R.

2 an binds fibronectin type III domains 3-5 of tenascin-R.

3 xtracellular matrix molecules tenascin-C and tenascin-R.

4 s that phosphacan forms a tight complex with tenascin-R.

5 expressed in the nervous system, also binds tenascin-R.

6 eceptors -1, -4, and -5, homer-1 and -2, and tenascin-R.

7 in domain of versican has been shown to bind tenascin-R, an extracellular matrix protein specifically

8 om adult rat brain extracts, suggesting that tenascin-R and brevican form complexes in vivo.

9 ping brain: the glycoproteins tenascin-C and tenascin-R and the chondroitin sulfate proteoglycans bre

10 phacan with the extracellular matrix protein tenascin-R and two heparin-binding proteins, amphoterin

11 We focused on aggrecan, brevican, and tenascin-R as they are especially expressed in the matur

12 We have determined that tenascin-R associated with Purkinje cell bodies and thei

13 fibronectin type III repeats 1-2 and 6-8 of tenascin-R but not to the epidermal growth factor-like d

14 The expression of tenascin-R by oligodendrocytes and small interneurons in

15 other lecticans also bind the same domain of tenascin-R by protein-protein interactions.

16 Versican and tenascin-R colocalized in OLCs, and coimmunoprecipitatio

17 resembled that in perineuronal nets in which tenascin-R has been localized.

18 with beta1,4-linked GalNAc-4-SO(4), whereas tenascin-R in other regions of the cerebellum does not b

19 omain of the beta2 subunit to tenascin-C and tenascin-R in vitro.

20 ough the fibronectin type III domains 3-5 of tenascin-R, independent of any carbohydrates or sulfated

21 The cellular adhesion molecule tenascin-R is a multifunctional extracellular matrix com

22 Tenascin-R is coprecipitated with brevican from adult ra

23 and suggest that brevican is a physiological tenascin-R ligand in the adult brain.

24 ular matrix molecules such as tenascin-C and tenascin-R may play a crucial role in localizing sodium

25 y reported interactions between brevican and tenascin-R may play a functional role within the perineu

26 tion of this unique sulfated carbohydrate to tenascin-R may serve to modulate its adhesive/anti-adhes

27 sed the effect of aggrecan, brevican, and/or tenascin-R on neurite outgrowth in vitro.

28 The 180-kDa core protein contains a tenascin-R-related molecule, consistent with recent obse

29 rotein expression of aggrecan, brevican, and tenascin-R throughout the rat brain utilizing immunohist

30 Tenascin-R (TN-R) is a member of the tenascin family of

31 f chondroitin sulfate proteoglycans (CSPGs), tenascin-R (TN-R), hyaluronan (HA), and link proteins, s

32 X (TNX), tenascin-C (TNC, or cytotactin) and tenascin-R (TN-R, or restrictin).

33 e of the purified proteins was identified as tenascin-R (TNR) by mass spectrometric analysis.

34 w that the extracellular matrix glycoprotein tenascin-R (TNR) is produced in the granule cell layer o

35 absence of calcium, binding of phosphacan to tenascin-R was not affected by the absence of divalent c

36 ontaining various segments of tenascin-C and tenascin-R were purified, digested with thrombin to remo

37 an immunoreactivity colocalized with that of tenascin-R, which was also substantially codistributed w

38 ans show saturable, high affinity binding to tenascin-R with apparent dissociation constants in the 2

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