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GoogleBot | / | ✔ |
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Title | Nathan |
Description | Research Overview History People Facilities Publications News Contact Menu NATHAN LAB Research Overview History People Facilities Publications News Contac |
Keywords | N/A |
WebSite | nathanlab.org |
Host IP | 198.185.159.145 |
Location | United States |
Site | Rank |
US$1,600,726
Last updated: 2022-10-09 08:28:38
nathanlab.org has Semrush global rank of 6,612,190. nathanlab.org has an estimated worth of US$ 1,600,726, based on its estimated Ads revenue. nathanlab.org receives approximately 184,700 unique visitors each day. Its web server is located in United States, with IP address 198.185.159.145. According to SiteAdvisor, nathanlab.org is safe to visit. |
Purchase/Sale Value | US$1,600,726 |
Daily Ads Revenue | US$1,478 |
Monthly Ads Revenue | US$44,328 |
Yearly Ads Revenue | US$531,934 |
Daily Unique Visitors | 12,314 |
Note: All traffic and earnings values are estimates. |
Host | Type | TTL | Data |
nathanlab.org. | A | 14400 | IP: 198.185.159.145 |
nathanlab.org. | A | 14400 | IP: 198.49.23.144 |
nathanlab.org. | A | 14400 | IP: 198.49.23.145 |
nathanlab.org. | A | 14400 | IP: 198.185.159.144 |
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Research Overview History People Facilities Publications News Contact Menu NATHAN LAB Research Overview History People Facilities Publications News Contact The Nathan lab is in the Department of Microbiology and Immunology at Weill Cornell Medicine in NYC. The lab studies host-pathogen interactions, focusing on macrophages and Mycobacterium tuberculosis (Mtb). Our projects today pursue the following topics: host pathways controlling susceptibility and resistance to Mtb; the genes on which Mtb depends to survive the stresses associated with aerosol transmission; the biology of Mtb in non-replicating (NR) states, during which the pathogen displays phenotypic resistance to conventionally developed antibiotics; and efforts to overcome Mtb’s phenotypic resistance by developing new antimicrobial agents. We are currently targeting two “hub” enzymes in Mtb—enzymes that participate in multiple functionally distinct complexes, such as lipoamide dehydrogenase, or control the activation of |
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