Localization of heat shock protein 110 in canine mammary gland tumors
Heat shock proteins (HSPs) function as molecular chaperones in the regulation of protein folding, conformation, and assembly; in addition, they also protect cells from protein–protein aggregation resulting from cellular stress. Recently, HSPs were shown to be overexpressed in several human cancer ce...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Okada, Satoru [verfasserIn] |
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Englisch |
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2015 |
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8 |
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Enthalten in: Mo1377 Safety and Effectiveness of Colorectal Endoscopic Submucosal Dissection in Elderly Patients: Clinical Outcomes Including Long-Term Follow-up - 2012, an international journal dealing with the study of veterinary immunology and immunopathology as applied to domestic animals, laboratory animals and other species that are useful to man, Amsterdam [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:167 ; year:2015 ; number:3 ; day:15 ; month:10 ; pages:139-146 ; extent:8 |
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| DOI / URN: |
10.1016/j.vetimm.2015.07.012 |
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ELV034406549 |
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| 520 | |a Heat shock proteins (HSPs) function as molecular chaperones in the regulation of protein folding, conformation, and assembly; in addition, they also protect cells from protein–protein aggregation resulting from cellular stress. Recently, HSPs were shown to be overexpressed in several human cancer cells compared with normal cells. HSPs are considered to be related to apoptosis-associated proteins, and inhibition of apoptosis promotes tumor growth. | ||
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Enthalten in Mo1377 Safety and Effectiveness of Colorectal Endoscopic Submucosal Dissection in Elderly Patients: Clinical Outcomes Including Long-Term Follow-up Amsterdam [u.a.] volume:167 year:2015 number:3 day:15 month:10 pages:139-146 extent:8 |
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Heat shock proteins (HSPs) function as molecular chaperones in the regulation of protein folding, conformation, and assembly; in addition, they also protect cells from protein–protein aggregation resulting from cellular stress. Recently, HSPs were shown to be overexpressed in several human cancer cells compared with normal cells. HSPs are considered to be related to apoptosis-associated proteins, and inhibition of apoptosis promotes tumor growth. |
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Heat shock proteins (HSPs) function as molecular chaperones in the regulation of protein folding, conformation, and assembly; in addition, they also protect cells from protein–protein aggregation resulting from cellular stress. Recently, HSPs were shown to be overexpressed in several human cancer cells compared with normal cells. HSPs are considered to be related to apoptosis-associated proteins, and inhibition of apoptosis promotes tumor growth. |
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Heat shock proteins (HSPs) function as molecular chaperones in the regulation of protein folding, conformation, and assembly; in addition, they also protect cells from protein–protein aggregation resulting from cellular stress. Recently, HSPs were shown to be overexpressed in several human cancer cells compared with normal cells. HSPs are considered to be related to apoptosis-associated proteins, and inhibition of apoptosis promotes tumor growth. |
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| title_short |
Localization of heat shock protein 110 in canine mammary gland tumors |
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https://doi.org/10.1016/j.vetimm.2015.07.012 |
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Furuya, Masaru Takenaka, Shigeo Fukui, Ayano Matsubayashi, Makoto Tani, Hiroyuki Sasai, Kazumi |
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Furuya, Masaru Takenaka, Shigeo Fukui, Ayano Matsubayashi, Makoto Tani, Hiroyuki Sasai, Kazumi |
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10.1016/j.vetimm.2015.07.012 |
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2024-07-06T21:02:41.389Z |
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