Results 71 to 80 of about 368,095 (294)

Biological, Serological and Molecular Characterization of Cucumber mosaic virus (CMV) Infecting Cucurbita moschata (Duchene ex. Poir) (Summer Squash) in Itu and Uyo Local Governments Areas, Akwa Ibom State, Nigeria

open access: yesAsian Journal of Biochemistry Genetics and Molecular Biology
Cucurbita moschata is an edible member of the family Cucurbitaceae. The plant is commonly observed showing typical virus-like symptoms during the growing season in Akwa Ibom State, Nigeria.
Daniel A. Usanga   +2 more
semanticscholar   +1 more source

Structural insights into lacto‐N‐biose I recognition by a family 32 carbohydrate‐binding module from Bifidobacterium bifidum

open access: yesFEBS Letters, EarlyView.
Bifidobacterium bifidum establishes symbiosis with infants by metabolizing lacto‐N‐biose I (LNB) from human milk oligosaccharides (HMOs). The extracellular multidomain enzyme LnbB drives this process, releasing LNB via its catalytic glycoside hydrolase family 20 (GH20) lacto‐N‐biosidase domain.
Xinzhe Zhang   +5 more
wiley   +1 more source

Yeasts [PDF]

open access: yes, 2018
Yeasts are a group of eukaryotic microfungi with a well-defined cell wall whose growth is either entirely unicellular or a combination of hyphal and unicellular reproduction. The approximately 1500 known yeast species belong to two distinct fungal phyla,
Lachance, Marc-Andre, Walker, Graeme M.
core   +2 more sources

The Caenorhabditis elegans DPF‐3 and human DPP4 have tripeptidyl peptidase activity

open access: yesFEBS Letters, EarlyView.
The dipeptidyl peptidase IV (DPPIV) family comprises serine proteases classically defined by their ability to remove dipeptides from the N‐termini of substrates, a feature that gave the family its name. Here, we report the discovery of a previously unrecognized tripeptidyl peptidase activity in DPPIV family members from two different species.
Aditya Trivedi, Rajani Kanth Gudipati
wiley   +1 more source

Gene expression patterns of sulfur starvation in Synechocystis sp. PCC 6803

open access: yesBMC Genomics, 2008
Background The unicellular cyanobacterium Synechocystis sp. PCC 6803 is a model microbe for studying biochemistry, genetics and molecular biology of photobiological processes.
Pendse Ninad D   +4 more
doaj   +1 more source

Proteomics: more than just biochemistry [PDF]

open access: yes
Growth of the so-called 'omics' technologies may appear to be simply a case of giving new, trendy names to boring, old-fashioned technology. After all, who would dispute that genomics is just genetics and molecular biology, glycomics is the study of ...
Greenwell, P.   +3 more
core  

Deciphering the genome structure and paleohistory of _Theobroma cacao_ [PDF]

open access: yes, 2010
We sequenced and assembled the genome of _Theobroma cacao_, an economically important tropical fruit tree crop that is the source of chocolate. The assembly corresponds to 76% of the estimated genome size and contains almost all previously described ...
Angé   +60 more
core   +2 more sources

Molecular bases of circadian magnesium rhythms across eukaryotes

open access: yesFEBS Letters, EarlyView.
Circadian rhythms in intracellular [Mg2+] exist across eukaryotic kingdoms. Central roles for Mg2+ in metabolism suggest that Mg2+ rhythms could regulate daily cellular energy and metabolism. In this Perspective paper, we propose that ancestral prokaryotic transport proteins could be responsible for mediating Mg2+ rhythms and posit a feedback model ...
Helen K. Feord, Gerben van Ooijen
wiley   +1 more source

Journal of Cellular and Molecular Medicine: the Future

open access: yesJournal of Cellular and Molecular Medicine, 2017
The field of Cellular and Molecular Medicine strives to understand the molecular basis of cell physiology and pathology, as well as cellular responses to extracellular stimuli.
S. Constantinescu
semanticscholar   +1 more source

Peptide‐based ligand antagonists block a Vibrio cholerae adhesin

open access: yesFEBS Letters, EarlyView.
The structure of a peptide‐binding domain of the Vibrio cholerae adhesin FrhA was solved by X‐ray crystallography, revealing how the inhibitory peptide AGYTD binds tightly at its Ca2+‐coordinated pocket. Structure‐guided design incorporating D‐amino acids enhanced binding affinity, providing a foundation for developing anti‐adhesion therapeutics ...
Mingyu Wang   +9 more
wiley   +1 more source

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