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Calpain.net lookup results from whois.godaddy.com server:
- Domain created: 2011-07-04T05:27:07Z
- Domain updated: 2023-06-30T11:18:54Z
- Domain expires: 2024-07-04T05:27:07Z 0 Years, 59 Days left
- Website age: 12 Years, 306 Days
- Registrar Domain ID: 1665146569_DOMAIN_NET-VRSN
- Registrar Url: http://www.godaddy.com
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- Registrar Abuse Contact Email: [email protected]
- Registrar Abuse Contact Phone: 480-624-2505
- Name server:
- NS15.ABOVEDOMAINS.COM
- NS16.ABOVEDOMAINS.COM
Administrator
- role : Trellian Pty Ltd administrator
- address : 8 East Concourse, Beaumaris Victoria 3193
- country : AU
- phone : +61395897946
- fax : +61395897946
- email : [email protected]
- admin-c : TPLA7-AP
- tech-c : TPLA7-AP
- handle : TPLA7-AP
- mnt-by : MAINT-TRELLIAN-AU
- last-modified : 2014-01-24T01:34:44Z
- source : APNIC
Technical support
- role : Trellian Pty Ltd administrator
- address : 8 East Concourse, Beaumaris Victoria 3193
- country : AU
- phone : +61395897946
- fax : +61395897946
- email : [email protected]
- admin-c : TPLA7-AP
- tech-c : TPLA7-AP
- handle : TPLA7-AP
- mnt-by : MAINT-TRELLIAN-AU
- last-modified : 2014-01-24T01:34:44Z
- source : APNIC
Network
- inetnum : 103.224.212.0 - 103.224.213.255
- name : TRELLIAN-AU
- country : AU
- org : ORG-TPL33-AP
- abuse-c : AT1100-AP
- status : ASSIGNED PORTABLE
- remarks : --------------------------------------------------------,To report network abuse, please contact mnt-irt,For troubleshooting, please contact tech-c and admin-c,Report invalid contact via www.apnic.net/invalidcontact,--------------------------------------------------------
- mnt-by : APNIC-HM
- mnt-routes : MAINT-TRELLIAN-AU
- mnt-irt : IRT-TRELLIAN-AU
- last-modified : 2020-11-25T06:34:10Z
- source : APNIC
Owner
- organization : Trellian Pty. Limited
- address : 8 East Concourse, Beaumaris Victoria 3193
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Host Informations
- IP address: 103.224.212.211
- Location: Australia
- Latitude: -33.494
- Longitude: 143.2104
- Timezone: Australia/Sydney
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Calpain - Wikipedia
A calpain is a protein belonging to the family of calcium-dependent, non-lysosomal cysteine proteases (proteolytic enzymes) expressed ubiquitously in mammals and many other organisms. Calpains constitute the C2 family of protease clan CA in the MEROPS database. The calpain proteolytic system includes the calpain proteases, the small regulatory subunit CAPNS1, also kno…
En.wikipedia.orgCalpain signaling: from biology to therapeutic opportunities in ...
Web Sep 5, 2023 · Calpain signaling, with its diverse roles in cellular processes, has attracted attention as a potential therapeutic target in these neurodegenerative diseases. This …
Ncbi.nlm.nih.govThe Critical Role of Calpain in Cell Proliferation - PMC
Web Aug 21, 2021 · Calpain are implicated in many physiological and pathological processes. They have significant role in the cell proliferation, differentiation and migration in a variety …
Ncbi.nlm.nih.govCalpain-2 as a therapeutic target for acute neuronal injury
Web Jan 18, 2021 · Expert opinion. As evidence accumulates that calpain-2 activation participates in acute neuronal injury, there is interest in developing therapeutic …
Ncbi.nlm.nih.govThe calpains: modular designs and functional diversity
Web Aug 6, 2007 · In mammals and plants it is clear that a calpain plays an essential role in development. There is increasing evidence that ubiquitous calpains participate in a variety of signal transduction pathways and …
Genomebiology.biomedcentral.comCalpain-1 and Calpain-2 in the Brain: New Evidence for a
Web Dec 16, 2020 · Calpains are a family of soluble calcium-dependent proteases that are involved in multiple regulatory pathways. Our laboratory has focused on the …
Pubmed.ncbi.nlm.nih.govThe calcium-dependent protease calpain in neuronal remodeling …
Web calcium homeostasis. ischemia. dendritic pruning. Calpains are cysteine proteases activated by Ca2+. Calpain was first discovered in 1964 during studies of proteolytic processes …
Cell.comHow calpain is activated by calcium - Nature
Web Apr 1, 2002 · Calpains are a family of cytosolic cysteine proteinases whose enzymatic activities depend on Ca 2+. Members of the calpain family are believed to function in …
Nature.comEffects of functionally diverse calpain system on immune cells
Web Jan 23, 2021 · Calpains are a family of nonlysosomal cysteine proteases, which play important roles in numerous physiological and pathological processes. Locations of them …
Link.springer.comThe calpain system - PubMed
Web Calpain. The calpain system originally comprised three molecules: two Ca2+-dependent proteases, mu-calpain and m-calpain, and a third polypeptide, calpastatin, whose only …
Pubmed.ncbi.nlm.nih.govThe calcium-dependent protease calpain in neuronal remodeling …
Web Neurosciences. Review. The calcium-dependent protease calpain in neuronal remodeling and neurodegeneration. Elsayed Metwally,1,2,3 Guoli Zhao,1,4 and Yong Q. Zhang1,2,* …
Cell.comCalpine | America’s Premier Power Generation Company
Web Calpine is America’s largest generator of electricity from natural gas and geothermal resources and one of the largest retail providers of power.
Calpine.comNylander, Lindholm exchange goals to open scoring in Game 7
Web 2 hours ago · Watch as Maple Leafs’ William Nylander opens the scoring in the third period, but loses the lead quickly with a game-tying goal by fellow Swede Hampus Lindholm.
Sportsnet.caCalpain-1 and Calpain-2 in the Brain: New Evidence for a Critical …
Web Dec 16, 2020 · Calpains are a family of soluble calcium-dependent proteases that are involved in multiple regulatory pathways. Our laboratory has focused on the …
Ncbi.nlm.nih.gov'Again...': Maple Leafs fans in shambles after another …
Web 1 hour ago · Maple Leafs fans in shambles after another heartbreaking end to season. Fans watch the Toronto Maple Leafs play the Boston Bruins in game 6 of first-round NHL …
Sportsnet.caCalpains: an elaborate proteolytic system - PubMed
Web Calpain is an intracellular Ca (2+)-dependent cysteine protease (EC 3.4.22.17; Clan CA, family C02). Recent expansion of sequence data across the species definitively shows …
Pubmed.ncbi.nlm.nih.gov
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