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MBL
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- Woods Hole also contains several scientific organizations such as the Woods Hole Oceanographic Institution (WHOI), the Marine Biological Laboratory (MBL), the Woodwell Climate Research Center, NOAA's Woods Hole Science Aquarium, and the scientific institutions' various museums.
- The MBL Library was established in 1889, with scientist and future MBL trustee Cornelia Clapp serving as librarian.
- These three traverses led to the discovery of the Bentley Subglacial Trench or Trough, a deep bedrock chasm between MBL and the Transantarctic Mountains of East Antarctica.
- Fungal pathogens such as Candida albicans and Cryptococcus neoformans as well as some viruses such as HIV-1 and Respiratory syncytial virus (RSV) are bound by MBL.
- When the carbohydrate-recognising heads of MBL bind to specifically arranged mannose residues on the surface of a pathogen, MASP-2 is activated to cleave complement components C4 and C2 into C4a, C4b, C2a, and C2b.
- Mannose-binding lectin (MBL), also called mannan-binding lectin or mannan-binding protein (MBP), is a lectin that is instrumental in innate immunity as an opsonin and via the lectin pathway.
- Unlike many individuals with lymphocytosis due to the latter disorders, individuals with MBL are asymptomatic, may have a family history of CLL/SLL, are usually >40 years old, and may have a history of serious infections (high-count MBL is ~3-fold more likely than age-matched healthy controls to have a history of serious infections and infection-related hospitalizations).
- MBL activates the complement lectin pathway by binding to glycoconjugates on the surface of a variety of clinically significant bacteria, viruses, and fungi that contain mannose, fucose, or N-acetylglucosamine.
- In the lectin pathway, aureolysin inhibits MBL and ficolin binding which, in turn, reduce C3b deposition.
- In 1984, upon completing his postdoctoral studies and returning to Israel, Boussiba joined the Microalgal Biotechnology Laboratory (MBL) at Jacob Blaustein Institutes for Desert Research BIDR, BGU.
- Analyses of genome sequences from Salisediminibacterium species identified four conserved signature indels (CSIs) for this genus in the following proteins: insulinase family protein, alpha-ketoacid dehydrogenase subunit beta, MBL fold metallo-hydrolase and excinuclease ABC subunit UvrA, which in most cases are exclusively shared by either all or most members of this genus.
- When considering eigenstate order in MBL systems, one generally speaks of highly excited eigenstates at energy densities that would correspond to high or infinite temperatures if the system were able to thermalize.
- Analyses of genome sequences from Ectobacillus have identified five conserved signature indels (CSIs) that are exclusive for Ectobacillus species in the proteins 3-isopropylmalate dehydratase small subunit, bacillithiol biosynthesis deacetylase BshB1, aldo or keto reductase, MBL fold metallo-hydrolase, and CYTH domain-containing protein.
- 14 CSIs have been identified for this genus in the proteins ABC transporter substrate-binding protein, helicase-exonuclease subunit AddAB subunit AddA, MFS transporter, 3-oxoacid CoA-transferase subunit B, LTA synthase family protein, sulphate ABC transporter permease subunit CysW, class I SAM-dependent RNA methyltransferase, site-specific tyrosine recombinase XerD, 3-isopropylmalate dehydrogenase, 5-oxoprolinase subunit PxpB, MATE family efflux transporter, ABC transporter permease, MBL fold metallo-hydrolase and YitT family protein and is in most cases shared by all members of this genus.
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