Results 1 to 10 of about 9,310 (182)

The Structural Properties of Odorants Modulate Their Association to Human Odorant Binding Protein [PDF]

open access: yesBiomolecules, 2021
The binding of known odorant molecules to the human odorant-binding protein (hOBP) was evaluated in silico. Docking experiments elucidate the preferable binding site and binding affinity of odorant molecules to hOBP.
Tarsila G. Castro   +3 more
doaj   +2 more sources

Ligand Binding Properties of Odorant-Binding Protein OBP5 from Mus musculus [PDF]

open access: yesBiology, 2022
Odorant-binding proteins (OBPs) are abundant soluble proteins secreted in the nasal mucus of a variety of species that are believed to be involved in the transport of odorants toward olfactory receptors.
Lucie Moitrier   +5 more
doaj   +2 more sources

Expression Profile and Ligand Screening of a Putative Odorant-Binding Protein, AcerOBP6, from the Asian Honeybee [PDF]

open access: yesInsects, 2021
Olfaction is essential in some behaviors of honeybee, such as nursing, foraging, attracting a mate, social communication, and kin recognition. OBPs (odorant binding proteins) play a key role in the first step of olfactory perception.
Huiting Zhao   +4 more
doaj   +2 more sources

Binding Properties of Odorant-Binding Protein 4 of Tirathaba rufivena to Areca catechu Volatiles [PDF]

open access: yesPlants, 2022
Odorant-binding proteins (OBPs) play a key role in the olfactory system and are essential for mating and oviposition host selection. Tirathaba rufivena, a serious lepidopterous insect pest of the palm area in recent years, has threatened cultivations of ...
Xiang Zhou   +7 more
doaj   +2 more sources

How allosteric mutations control ligand binding in Lipocalin protein: odorant binding protein as a test case [PDF]

open access: yesCellular and Molecular Life Sciences
Lipocalins are a family of proteins found in mammals that are essential for the binding and transport of various molecules, but the mechanisms underlying their target recognition are still unclear.
Maxence Lalis   +11 more
doaj   +2 more sources

Pleiotropic fitness effects of a Drosophila odorant-binding protein [PDF]

open access: yesG3: Genes, Genomes, Genetics, 2022
Insect odorant-binding proteins (OBPs) are members of a rapidly evolving multigene family traditionally thought to facilitate chemosensation. However, studies on DrosophilaObp56hD.
Sneha S Mokashi   +4 more
doaj   +2 more sources

Functional characteristics of a novel odorant binding protein in the legume pod borer, Maruca vitrata [PDF]

open access: yesScientific Reports, 2021
Insect olfaction system plays a key role in the foraging food, pollination, mating, oviposition, reproduction and other insect physiological behavior. Odorant binding protein are widely found in the various olfactory sensilla of different insect antennae
Hui Ai   +5 more
doaj   +2 more sources

Molecular and cellular organization of odorant binding protein genes in Drosophila [PDF]

open access: yesHeliyon
Chemosensation is important for the survival and reproduction of animals. The odorant binding proteins (OBPs) are thought to be involved in chemosensation together with chemosensory receptors.
Keehyun Park   +11 more
doaj   +2 more sources

The diverse small proteins called odorant-binding proteins [PDF]

open access: yesOpen Biology, 2018
The term ‘odorant-binding proteins (Obps)’ is used to refer to a large family of insect proteins that are exceptional in their number, abundance and diversity. The name derives from the expression of many family members in the olfactory system of insects
Jennifer S. Sun   +2 more
doaj   +3 more sources

Biological Roles of Lipocalins in Chemical Communication, Reproduction, and Regulation of Microbiota

open access: yesFrontiers in Physiology, 2021
Major evolutionary transitions were always accompanied by genetic remodelling of phenotypic traits. For example, the vertebrate transition from water to land was accompanied by rapid evolution of olfactory receptors and by the expansion of genes encoding
Romana Stopková   +4 more
doaj   +1 more source

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