Results 71 to 80 of about 3,908,770 (297)

Evaluating the involvement of autolysosomes in the nuclear translocation of fluorescent proteins

open access: yesFEBS Open Bio, EarlyView.
Endogenously expressed fluorescent proteins can be degraded by autophagy and transported to cell nuclei via the nuclear pore complex. But in some cell lines, for example, HeLa cells which are positive for immunoreactivity of a receptor ligand, such as UCN I, in cell nuclei, fusion of autolysosome with the nuclear envelope is involved in the nuclear ...
Keiichi Ikeda
wiley   +1 more source

Mechanism of Protein Transport across the Chloroplast Envelope [PDF]

open access: yesPlant Physiology, 1997
info:eu-repo/semantics ...
Fuks, Bruno, Schnell, Danny D.J.
openaire   +3 more sources

Loss of AMBRA1 activates MAPK and angiogenesis signaling pathways in melanoma cells

open access: yesFEBS Open Bio, EarlyView.
Loss of AMBRA1 in melanoma cells activates multiple oncogenic pathways associated with tumor progression. Transcriptomic and protein network analyses revealed that AMBRA1 depletion enhances MAPK/ERK signaling, angiogenesis, TGF‐β/EMT signaling, and Wnt/axon guidance pathways.
Milad Ibrahim   +4 more
wiley   +1 more source

Relatedness of baculovirus and gypsy retrotransposon envelope proteins [PDF]

open access: yesBMC Evolutionary Biology, 2001
Current evidence suggests that lepidopteran baculoviruses may be divided into two phylogenetic groups based on their envelope fusion proteins. One group utilizes gp64, a low pH-dependent envelope fusion protein, whereas the other employs a protein family (e.g.
Karplus P Andrew, Rohrmann George F
openaire   +3 more sources

The gateway to chloroplast: re-defining the function of chloroplast receptor proteins [PDF]

open access: yes, 2012
Chloroplast biogenesis often requires a tight orchestration between gene expression (both plastidial and nuclear) and translocation of similar to 3000 nuclear-encoded proteins into the organelle.
Bölter, Bettina   +2 more
core   +1 more source

Importin 7 mediates the nuclear import of HIV‐1 integrase via a specific interacting interface

open access: yesFEBS Open Bio, EarlyView.
HIV‐1 integrase enables viral DNA integration into the host genome. By binding to the core domain of the host protein Importin 7 via its C‐terminal domain, the integrase is transported across the nuclear membrane into the nucleus, where integration of the viral genome into host DNA takes place. This translocation is a critical step for subsequent viral
Juana Bana   +5 more
wiley   +1 more source

Studying protein-protein interactions using peptide arrays [PDF]

open access: yes, 2010
Screening of arrays and libraries of compounds is well-established as a high-throughput method for detecting and analyzing interactions in both biological and chemical systems. Arrays and libraries can be composed from various types of molecules, ranging
Rito, T.   +7 more
core   +1 more source

Threonine 348 regulates the subcellular localization of PTEN

open access: yesFEBS Open Bio, EarlyView.
Thr348 in the C2 domain is a key contributor to PTEN subcellular localization. The PTEN350 fragment and PTENA4 accumulated in the nucleus, whereas PTENK13R,A4 predominantly localized to the plasma membrane. In contrast, substitution of Thr348 with Asp (T348D) disrupted these characteristic localization patterns, resulting in predominant cytoplasmic ...
Takashi Kato, Suzu Tanaka, Miyu Ohashi
wiley   +1 more source

Identification and characterization of key residues in Zika virus envelope protein for virus assembly and entry

open access: yesEmerging Microbes and Infections, 2022
Zika virus (ZIKV), a family member in the Flavivirus genus, has re-emerged as a global public health concern. The envelope (E) proteins of flaviviruses play a dual role in viral assembly and entry.
Xiao Ma, Zhenghong Yuan, Zhigang Yi
doaj   +1 more source

Envelope membrane proteins that interact with chloroplastic precursor proteins. [PDF]

open access: yesThe Plant Cell, 1994
The post-translational transport of cytoplasmically synthesized precursor proteins into chloroplasts requires proteins in the envelope membranes. To identify some of these proteins, label transfer cross-linking was performed using precursor to the small subunit of ribulose-1,5-bisphosphate carboxylase (prSSU) that was blocked at an early stage of the ...
S E, Perry, K, Keegstra
openaire   +2 more sources

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