Results 101 to 110 of about 5,115,827 (299)

Eukaryotic protein production in designed storage organelles

open access: yesBMC Biology, 2009
Background Protein bodies (PBs) are natural endoplasmic reticulum (ER) or vacuole plant-derived organelles that stably accumulate large amounts of storage proteins in seeds. The proline-rich N-terminal domain derived from the maize storage protein γ zein
Saloheimo Markku   +9 more
doaj   +1 more source

The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer

open access: yesMolecular Oncology, EarlyView.
Mutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Lara Abad   +2 more
wiley   +1 more source

Bacterial expression and purification of recombinant Plasmodium yoelii circumsporozoite protein

open access: yes, 1997
We report the expression and purification of recombinant rodent malarialPlasmodium yoeliicircumsporozoite surface protein (PyCSP) inEscherichia coli.To facilitate purification of the recombinant protein, the PyCSP was expressed as an amino-terminal ...
Kang, A.S.   +3 more
core   +1 more source

Endotoxin Deactivation by Transient Acidification

open access: yesCell Transplantation, 2010
Recombinant proteins are an important tool for research and therapeutic applications. Therapeutic proteins have been delivered to several cell types and tissues and might be used to improve the outcome of the cell transplantation.
Melina M. Ribeiro   +6 more
doaj   +1 more source

SPHINX31 acts as a SRPK1 inhibitor targeting the ATR/DNA‐PKcs/CHK1 replicative checkpoint to inhibit cell growth in non‐small cell lung cancer

open access: yesMolecular Oncology, EarlyView.
The kinase SRPK1 directly interacts with the protein TOPBP1 and regulates the pre‐mRNA splicing of WIZ thereby contributing to the activation of the ATR/CHK1 replicative checkpoint in response to replicative stress. This allows cancer cells' genomic stability and survival.
Amani Shreim   +17 more
wiley   +1 more source

Mutant p53R273H disrupts PDPK1 homodimerization and contributes to PDPK1 activation

open access: yesMolecular Oncology, EarlyView.
How mutant p53R273H drives AKT signaling is unclear. We show that p53R273H, but not wild‐type, directly binds PDPK1 via a mutation‐dependent conformational change. This interaction disrupts inhibitory PDPK1 homodimerization and enhances AKT phosphorylation.
Mei Chee Lim   +11 more
wiley   +1 more source

Internship and postgraduate entrance examination: A qualitative study on the psychological experience of undergraduate nursing students under dual pressure in China

open access: yesHeliyon
Background: With the development of nursing positions and nursing disciplines in China's tertiary hospitals, the number of people applying for the master's degree in nursing is also increasing year by year.
Minghao Zhang   +7 more
doaj   +1 more source

Recombinant Protein Expression at the Zurich University of Applied Sciences Winterthur

open access: yesCHIMIA, 2002
In recent years recombinant enzymes have found widespread application in industrial uses ranging from organic synthesis to food industry. Recombinant proteins, including some enzymes, are nowadays used in the clinic to treat a broad spectrum of ...
Christiane Zaborosch
doaj   +1 more source

Molecular characterization of covRS mutations in M1UK Streptococcus pyogenes

open access: yesFEBS Open Bio, EarlyView.
Group A Streptococcus (GAS) acquires covRS mutations driving a hypervirulent bacterial state, frequently associated with invasive disease‐like necrotizing fasciitis. We demonstrate that the newly emerged M1UK GAS lineage can also acquire these mutations.
Jarrad Pritchard   +12 more
wiley   +1 more source

Synthesis and structural characterization of a mimetic membrane-anchored prion protein [PDF]

open access: yes, 2006
During pathogenesis of transmissible spongiform encephalopathies (TSEs) an abnormal form (PrPSc) of the host encoded prion protein (PrPC) accumulates in insoluble fibrils and plaques. The two forms of PrP appear to have identical covalent structures, but
Hicks, M R   +13 more
core   +1 more source

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