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There are several matches for 'hslO'.
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3027 matches
showing page 1 of 152
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organism
protein
1)
Escherichia coli K12
hslO
- Heat shock protein Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
2)
Homo sapiens
KCNMA1 - Calcium-activated potassium channel subunit alpha-1; Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in t [...]
[a.k.a. ENST00000640626, ENST00000286628, ENSP00000490881,
hSlo
]
3)
Abiotrophia defectiva
hslO
- Chaperonin
HslO
; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
4)
Absiella dolichum
hslO
- Chaperonin
HslO
; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
5)
Acaryochloris marina
hslO
- Chaperonin HSP33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
6)
Accumulibacter sp. BA92
hslO
- Heat shock protein 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family.
7)
Accumulibacter sp. BA93
hslO
- Heat shock protein 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family.
8)
Accumulibacter sp. BA94
hslO
- Heat shock protein 33.
9)
Accumulibacter sp. SK01
hslO
- Heat shock protein 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family.
10)
Accumulibacter sp. SK02
hslO
- Heat shock protein 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family.
11)
Accumulibacter sp. SK11
hslO
- Heat shock protein 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family.
12)
Accumulibacter sp. SK12
hslO
- Heat shock protein 33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family.
13)
Acetanaerobacterium elongatum
hslO
- Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
14)
Acetitomaculum ruminis
hslO
- Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
15)
Acetivibrio ethanolgignens
hslO
- Heat-shock protein Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
16)
Acetoanaerobium sticklandii
hslO
- Disulfide bond chaperone (heat shock protein HSP33); Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
17)
Acetobacter ghanensis
hslO
- Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family.
18)
Acetobacterium bakii
hslO
- Heat shock protein Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
19)
Acetobacterium wieringae
hslO
- 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
20)
Acetobacterium woodii
hslO
- 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
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