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Bee pollen is consumed for its nutritional and pharmacological benefits, but it also contains hazardous allergens which has not been identified. Here, we identified 2 potential allergens, glutaredoxin and oleosin-B2, in Brassica napus (B. napus) bee pollen using mass spectrometr...

2022-03-23 | MTBLS3950 | MetaboLights
Temperature plays an important role in the growth and development of lettuce (Lactuca sativa L.). A high temperature can induce bolting, which decreases both the quality and production of lettuce. However, knowledge of underlying lettuce bolting is still lacking, especially in the molecular basis th...
ORGANISM(S): Lactuca Sativa Var. Capitata 
Honeybee brain has distHoneybee brain has distinct anatomical and functional regions, knowledge on molecular underpinnings of sub-organ to achieve the distinct neural function and the difference between the eastern and western honeybees are still missing. Here, the proteomes of three sub-organs of e...
ORGANISM(S): Apis mellifera (Honeybee) 
2017-12-04 | PXD007091 | Pride
To identify the potential proteins from bee pollen of Brassica by proteomics approach
ORGANISM(S): Brassica Napus 
2021-12-09 | PXD030273 |
Decipher molecular mechanism underpinning important honeybee biology such as royal jelly production using proteomics, genomics and gene editing protocols
ORGANISM(S): Apis Mellifera 
2020-06-09 | PXD019657 |
Using honey bee (Apis mellifera) as a model, we confirmed that honeybee queens with big ovaries lay smaller eggs in colonies with more worker bees.
ORGANISM(S): Apis Mellifera 
2021-11-22 | PXD029859 |
The neuronal basis of complex social behavior is still poorly understood. In honeybees, reproductive investment decisions are made at the colony-level. Queens develop from female-destined larvae that receive alloparental care from nurse bees in the form of ad-libitum royal jelly (RJ) secretions. Typ...
ORGANISM(S): Apis Mellifera 
By using Limited Proteolysis-Mass Spectrometry (LiP-MS) and Hydrogen Deuterium Exchange-Mass Spectrometry (HDX-MS) analysis, we identified the binding pocket of Nec-34 in RIPK1 kinase domain. This newly identified binding pocket of Nec-34 is distinct from distinct from that of Nec-1s.
ORGANISM(S): Homo Sapiens 
2021-03-07 | PXD024560 |
We identified a peptide of RIPK1 binding with compound Nec-34
ORGANISM(S): Homo Sapiens 
2021-03-04 | PXD024534 |
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