sameAs
Phenethyl isothiocyanate inhibits shiga toxin production in enterohemorrhagic Escherichia coli by stringent response induction.Diallyl trisulfide-induced G2/M phase cell cycle arrest in DU145 cells is associated with delayed nuclear translocation of cyclin-dependent kinase 1.Signal transduction pathways leading to cell cycle arrest and apoptosis induction in cancer cells by Allium vegetable-derived organosulfur compounds: a review.Diallyl trisulfide-induced prostate cancer cell death is associated with Akt/PKB dephosphorylation mediated by P-p66shc.Antibacterial and anticancer activities of acetone extracts from in vitro cultured lichen-forming fungiIsothiocyanates as effective agents against enterohemorrhagic Escherichia coli: insight to the mode of action.Sensitization of estrogen receptor-positive breast cancer cell lines to 4-hydroxytamoxifen by isothiocyanates present in cruciferous plants.Molecular targets of cancer chemoprevention by garlic-derived organosulfides.Replicating DNA by cell factories: roles of central carbon metabolism and transcription in the control of DNA replication in microbes, and implications for understanding this process in human cellsSulforaphane inhibits growth of phenotypically different breast cancer cells.Cellular responses to cancer chemopreventive agent D,L-sulforaphane in human prostate cancer cells are initiated by mitochondrial reactive oxygen species.Combination of lapatinib with isothiocyanates overcomes drug resistance and inhibits migration of HER2 positive breast cancer cells.The cell surface protein Ag43 facilitates phage infection of Escherichia coli in the presence of bile salts and carbohydrates.Sulforaphene, an isothiocyanate present in radish plants, inhibits proliferation of human breast cancer cells.Selective inhibition of cancer cells' proliferation by compounds included in extracts from Baltic Sea cyanobacteria.Sensitization of HER2 Positive Breast Cancer Cells to Lapatinib Using Plants-Derived Isothiocyanates.S6K1 controls autophagosome maturation in autophagy induced by sulforaphane or serum deprivation.Sulforaphane, a cruciferous vegetable-derived isothiocyanate, inhibits protein synthesis in human prostate cancer cells.Impact of JNK1, JNK2, and ligase Itch on reactive oxygen species formation and survival of prostate cancer cells treated with diallyl trisulfide.P66Shc mediated ferritin degradation--a novel mechanism of ROS formation.Molecular mechanism of heat shock-provoked disassembly of the coliphage lambda replication complex.NADH-generating substrates reduce peroxyl radical toxicity in RL-34 cells.Tumor necrosis factor-alpha-induced reactive oxygen species formation is mediated by JNK1-dependent ferritin degradation and elevation of labile iron pool.Induction of p21 protein protects against sulforaphane-induced mitotic arrest in LNCaP human prostate cancer cell line.Activation of a novel ataxia-telangiectasia mutated and Rad3 related/checkpoint kinase 1-dependent prometaphase checkpoint in cancer cells by diallyl trisulfide, a promising cancer chemopreventive constituent of processed garlic.D,L-Sulforaphane-induced cell death in human prostate cancer cells is regulated by inhibitor of apoptosis family proteins and Apaf-1.Sulforaphane causes autophagy to inhibit release of cytochrome C and apoptosis in human prostate cancer cells.c-Jun NH(2)-terminal kinase signaling axis regulates diallyl trisulfide-induced generation of reactive oxygen species and cell cycle arrest in human prostate cancer cells.Checkpoint kinase 1 regulates diallyl trisulfide-induced mitotic arrest in human prostate cancer cells.Diallyl trisulfide-induced G(2)-M phase cell cycle arrest in human prostate cancer cells is caused by reactive oxygen species-dependent destruction and hyperphosphorylation of Cdc 25 C.Sulforaphane-induced cell death in human prostate cancer cells is initiated by reactive oxygen species.Influence of the Escherichia coli oxyR gene function on lambda prophage maintenance.PrpE, a PPP protein phosphatase from Bacillus subtilis with unusual substrate specificity.The C-terminal domain of the Escherichia coli RNA polymerase alpha subunit plays a role in the CI-dependent activation of the bacteriophage lambda pM promoter.A plasmid cloning vector with precisely regulatable copy number in Escherichia coli.Sulforaphane-induced G2/M phase cell cycle arrest involves checkpoint kinase 2-mediated phosphorylation of cell division cycle 25C.Erratum to: Sulforaphane inhibits growth of phenotypically different breast cancer cells.4-(Methylthio)butyl isothiocyanate inhibits the proliferation of breast cancer cells with different receptor status.Genetic analysis of bacteriophage lambdaN-dependent antitermination suggests a possible role for the RNA polymerase alpha subunit in facilitating specific functions of NusA and NusE.Regulation of the switch from early to late bacteriophage λ DNA replication
P50
Q33623008-B25BFEB8-D328-4ACE-A827-77FEFF62C7E4Q33862448-425156E8-6791-44F3-A907-0018797782E5Q35914361-EAF77440-2C6B-4312-96B9-58B65F1529B9Q36275402-D981C651-CFFA-43E8-BFF8-9E6C76B9926FQ36395343-B49E4AB5-621F-45C1-8E66-87F8C417BFF5Q36628246-96A4D203-100E-4337-87C0-59B5FF33FCDAQ36762899-34133947-5DD6-4171-9C11-F6CC467F5BE3Q36920765-C3CBA06A-962D-46F3-A2B1-B762996CE7CAQ36972796-6FCE2F99-0B0C-45DE-8BD4-481067450172Q37321702-70B23047-240E-4798-BBE4-AB3C95FC6E67Q37347093-7D23F57F-B5A9-480F-8F4A-42B5AD2B6511Q37653981-214A603A-13F8-4AB0-94E5-4898DBE321AFQ38289611-F1103A3A-148B-4B9E-8DDA-1988D4AB9A88Q38703194-95CC4C5F-1097-40AF-82A8-49494379E4C7Q38832145-E0913F56-0C0D-4C74-BD06-8F70D95EE06DQ38857859-432A784C-D27A-407F-BE88-9061B3FF7FEAQ38866289-34015F8D-AA91-4DF0-B896-E92662C65242Q39341072-4FEE92B9-06AA-4E58-AE69-9126F7A59449Q39485547-EC8BA910-4033-4D5F-8778-A448BB11DBA3Q39535854-C79EF883-DF55-462A-B3DA-7CA937B7B759Q39565853-1C4647DB-13CD-4B3F-9E82-7D5CF407AA6FQ39768999-7286B52D-9F34-4787-A566-986CA3F23727Q40113023-E75B9D5D-8510-4359-BDC6-5DDCF2AE1FD1Q40130426-982A6B3E-6552-4C05-8B24-3F645B635E99Q40150178-C2A22032-A921-4F54-8223-46F7F661E97BQ40241718-167CF757-E702-4BB1-B1BE-DFE5DCF10433Q40272756-9D8ECCDC-9FA1-460C-8115-A39122DE5049Q40278650-2A58A9A6-5259-430A-9CBA-DE42D5157F01Q40408481-E0774368-DE3E-4297-94BF-5578D7AD3B90Q40412855-447DC238-CFC3-458C-8E6A-E336B8587721Q40447260-926546D0-2F9B-4614-895A-E4B2AA3BA7C5Q41895322-CC222F98-C31F-419F-B00F-16219471F153Q42073266-A90AE5D2-B2AD-4B10-8DCA-1A608AB98C30Q42779814-A3C0B5AE-974A-4B71-9F95-8D02EBE8BCCCQ43659373-5CF5DCFA-4BC2-4316-BDBA-DDB2A8797386Q44836647-CA30E0D6-0212-4453-9B01-644BD8FCA2DFQ46717371-F17441CC-24C7-4054-BE6B-8FF648E1D49BQ47730029-FC138B42-37BE-46FB-A55C-DBE273D865FFQ54522239-5B09B040-3052-46C2-B4BF-9714A8C11EC1Q63477445-7311C0BA-44B0-4C7B-A01C-0A8C5CE02831
P50
description
Polish molecular biologist
@en
Pools biologe
@nl
bitheolaí móilíneach Polannach
@ga
bióloga polaca
@ast
polska biolog molekularna
@pl
name
Anna Herman-Antosiewicz
@ast
Anna Herman-Antosiewicz
@ca
Anna Herman-Antosiewicz
@cs
Anna Herman-Antosiewicz
@de
Anna Herman-Antosiewicz
@en
Anna Herman-Antosiewicz
@es
Anna Herman-Antosiewicz
@fr
Anna Herman-Antosiewicz
@ga
Anna Herman-Antosiewicz
@gl
Anna Herman-Antosiewicz
@hr
type
label
Anna Herman-Antosiewicz
@ast
Anna Herman-Antosiewicz
@ca
Anna Herman-Antosiewicz
@cs
Anna Herman-Antosiewicz
@de
Anna Herman-Antosiewicz
@en
Anna Herman-Antosiewicz
@es
Anna Herman-Antosiewicz
@fr
Anna Herman-Antosiewicz
@ga
Anna Herman-Antosiewicz
@gl
Anna Herman-Antosiewicz
@hr
prefLabel
Anna Herman-Antosiewicz
@ast
Anna Herman-Antosiewicz
@ca
Anna Herman-Antosiewicz
@cs
Anna Herman-Antosiewicz
@de
Anna Herman-Antosiewicz
@en
Anna Herman-Antosiewicz
@es
Anna Herman-Antosiewicz
@fr
Anna Herman-Antosiewicz
@ga
Anna Herman-Antosiewicz
@gl
Anna Herman-Antosiewicz
@hr
P1412
P1559
Anna Herman-Antosiewicz
@pl
P19
P21
P214
300144647702000048245
P27
P2798
P31
P3124
P496
0000-0003-0526-2168
P569
1970-09-21T00:00:00Z
P735
P7859
viaf-300144647702000048245