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Nierenfunktion Kinase-defizienter Mäuse

von Dr. Diana Sandulache

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[1.] Dsa/Fragment 042 00 - Diskussion
Zuletzt bearbeitet: 2016-08-27 21:14:13 WiseWoman
Dsa, Fragment, Gesichtet, Hoenderop et al 2005, SMWFragment, Schutzlevel sysop, Verschleierung

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Hindemith
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Seite: 42, Zeilen: figure
Quelle: Hoenderop et al 2005
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Dsa 42a diss.png

Figure nr. 10 - TRP family with its subgroups.

The vanilloids, the classical, the melastatin, the mucolipins (TRPML) and the polycystins (TRPP) (members of TRPN, TRPA not shown).

Dsa 42a source2.jpg

Fig. 2.

Mammalian TRP family tree. The evolutionary distance between the TRP channels is shown by the total branch lengths in point accepted mutations (PAM) units, which is the mean number of substitutions per 100 residues. The tree was calculated using the neighbor-joining method for human, rat, and mouse sequences. [From Clapham (74).]

Anmerkungen

Saparov 2007 is the source for the entire page, but it is only available in the Internet Archives without the illustrations. Saparov gives Hoenderop et al 2005 as the source for this illustration, and it is identical, although the caption in Dsa is the caption from Saparov 2007 and not the caption from Hoenderop et al 2005.

Sichter
(Hindemith), WiseWoman

[2.] Dsa/Fragment 042 01 - Diskussion
Zuletzt bearbeitet: 2016-08-27 21:21:08 WiseWoman
Dsa, Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Saparov 2007, Schutzlevel sysop

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Transient receptor potential channels (TRPs)

The mammalian TRP channels encode a family of about 30 ion channel proteins. This superfamily consists of seven diverse groups structurally similar to the originally found Drosophila TRP and they differ in ion selectivities, modes of activation and physiological functions.


[Figure nr 10]

Figure nr. 10 - TRP family with its subgroups. The vanilloids, the classical, the melastatin, the mucolipins (TRPML) and the polycystins (TRPP) (members of TRPN, TRPA not shown).

TRP proteins are expressed predominantly in the nervous system and are of particular importance in sensory physiology. (Montell C. et al., (2005) Sci STKE).

In each subfamily are three to eight members. (Hönderop JG. et al., (2005) Physiol Rev). The reason to identify mammalian TRPs is to characterize those channels that might account for highly Ca2+ selective Ca2+ entry mechanism in nonexcitable cells, referred to as store-operated Ca2+ entry (SOCE). SOCE is interesting, due to association of these modes of Ca2+ entry with processes ranging from T cell activation to apoptosis, cell proliferation, fluid secretion and cell migration.(Montell C. et al., (2005) Sci STKE.). The TRP superfamily can be divided into two structurally different groups (Clapham DE. et al., (2003) Pharmacol Rev):

Group 1: TRPC, TRPV, TRPM, TRPN, TRPA. They share substantial sequence identity in the transmembrane domains.

Group 2: TRPP and TRPML. They have low sequence similarity and a large extracellular loop between the first and the second transmembrane domains.

Transient receptor potential channels (TRPs)

The mammalian TRP channels encode a family of about 30 ion channel proteins. This superfamily consists of seven diverse groups structurally similar to the originally found Drosophila TRP and they differ in ion selectivities, modes of activation and physiological functions. TRP proteins are expressed predominantly in the nervous system and are of particular importance in sensory physiology. (1)

[Illustration] Summary of the different TRP family members

TRP family with its subgroups: the vanilloids, the classical, the melastatin, the mucolipins (TRPML) and the polycystins (TRPP) (members of TRPN, TRPA not shown). In each subfamily are three to eight members. (2)

The reason to identify mammalian TRPs is to characterize those channels that might account for highly Ca2+ selective Ca2+ entry mechanism in nonexcitable cells, referred to as store-operated Ca2+ entry (SOCE). SOCE is interesting, due to association of these modes of Ca2+ entry with processes ranging from T cell activation to apoptosis, cell proliferation, fluid secretion and cell migration.(1)

The TRP superfamily can be divided into two structurally different groups(1,3):

1. Group 1: TRPC, TRPV, TRPM, TRPN, TRPA They share substantial sequence identity in the transmembrane domains.

2. Group 2: TRPP and TRPML They have low sequence similarity and a large extracellular loop between the first and the second transmembrane domains.


1. Montell, C. (2005) Sci STKE 2005, re3

2. Hoenderop, J. G., Nilius, B., and Bindels, R. J. (2005) Physiol Rev 85, 373-42

3. Clapham, D. E., Montell, C., Schultz, G., and Julius, D. (2003) Pharmacol Rev 55, 591-596

Anmerkungen

The source is not given

Sichter
(WiseWoman), Hindemith


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