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Article ; Online: Bidirectional lysosome transport: a balancing act between ARL8 effectors.

Kendrick, Agnieszka A / Christensen, Jenna R

2022 Volume 13, Issue 1, Page(s) 5261

MeSH term(s)	ADP-Ribosylation Factors/metabolism ; Biological Transport ; Lysosomes/metabolism
Chemical Substances	ADP-Ribosylation Factors (EC 3.6.5.2)
Language	English
Publishing date	2022-09-07
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-022-32965-y
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Article ; Online: Lis1 relieves cytoplasmic dynein-1 autoinhibition by acting as a molecular wedge.

Karasmanis, Eva P / Reimer, Janice M / Kendrick, Agnieszka A / Nguyen, Kendrick H V / Rodriguez, Jennifer A / Truong, Joey B / Lahiri, Indrajit / Reck-Peterson, Samara L / Leschziner, Andres E

Nature structural & molecular biology

2023 Volume 30, Issue 9, Page(s) 1357–1364

Abstract: Cytoplasmic dynein-1 transports intracellular cargo towards microtubule minus ends. Dynein is autoinhibited and undergoes conformational changes to form an active complex that consists of one or two dynein dimers, the dynactin complex, and activating ... ...

Abstract	Cytoplasmic dynein-1 transports intracellular cargo towards microtubule minus ends. Dynein is autoinhibited and undergoes conformational changes to form an active complex that consists of one or two dynein dimers, the dynactin complex, and activating adapter(s). The Lissencephaly 1 gene, LIS1, is genetically linked to the dynein pathway from fungi to mammals and is mutated in people with the neurodevelopmental disease lissencephaly. Lis1 is required for active dynein complexes to form, but how it enables this is unclear. Here, we present a structure of two yeast dynein motor domains with two Lis1 dimers wedged in-between. The contact sites between dynein and Lis1 in this structure, termed 'Chi,' are required for Lis1's regulation of dynein in Saccharomyces cerevisiae in vivo and the formation of active human dynein-dynactin-activating adapter complexes in vitro. We propose that this structure represents an intermediate in dynein's activation pathway, revealing how Lis1 relieves dynein's autoinhibited state.
MeSH term(s)	Animals ; Humans ; Cytoplasmic Dyneins/genetics ; Dyneins ; Classical Lissencephalies and Subcortical Band Heterotopias ; Biological Transport ; Cytoskeleton ; Dynactin Complex ; Oligonucleotides ; Mammals
Chemical Substances	Cytoplasmic Dyneins (EC 3.6.4.2) ; Dyneins (EC 3.6.4.2) ; Dynactin Complex ; Oligonucleotides
Language	English
Publishing date	2023-08-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2126708-X
ISSN	1545-9985 ; 1545-9993
ISSN (online)	1545-9985
ISSN	1545-9993
DOI	10.1038/s41594-023-01069-6
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Article ; Online: Overstretched and overlooked: solving challenges faced by early-career investigators after the pandemic.

Humphries, Brock A / Hwang, Priscilla Y / Kendrick, Agnieszka A / Kulkarni, Rajan P / Pozzar, Rachel A / San Martin, Rebeca

Trends in cancer

2021 Volume 7, Issue 10, Page(s) 879–882

Abstract: The coronavirus disease 2019 (COVID-19) pandemic has had a detrimental effect on research. However, little has been done to identify and solve the unique challenges faced by early career investigators (ECIs). As a group of American Cancer Society-funded ... ...

Abstract	The coronavirus disease 2019 (COVID-19) pandemic has had a detrimental effect on research. However, little has been done to identify and solve the unique challenges faced by early career investigators (ECIs). As a group of American Cancer Society-funded ECIs, we provide recommendations for solving these challenges in the aftermath of the pandemic.
MeSH term(s)	COVID-19 ; Career Mobility ; Humans ; Mentoring ; Research Personnel/economics ; Societies, Scientific ; Work-Life Balance
Language	English
Publishing date	2021-08-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	2852626-0
ISSN	2405-8025 ; 2405-8033 ; 2405-8033
ISSN (online)	2405-8025 ; 2405-8033
ISSN	2405-8033
DOI	10.1016/j.trecan.2021.07.005
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Article ; Online: Cytoplasmic dynein-1 cargo diversity is mediated by the combinatorial assembly of FTS-Hook-FHIP complexes.

Christensen, Jenna R / Kendrick, Agnieszka A / Truong, Joey B / Aguilar-Maldonado, Adriana / Adani, Vinit / Dzieciatkowska, Monika / Reck-Peterson, Samara L

eLife

2021 Volume 10

Abstract: In eukaryotic cells, intracellular components are organized by the microtubule motors cytoplasmic dynein-1 (dynein) and kinesins, which are linked to cargos via adaptor proteins. While ~40 kinesins transport cargo toward the plus end of microtubules, a ... ...

Abstract	In eukaryotic cells, intracellular components are organized by the microtubule motors cytoplasmic dynein-1 (dynein) and kinesins, which are linked to cargos via adaptor proteins. While ~40 kinesins transport cargo toward the plus end of microtubules, a single dynein moves cargo in the opposite direction. How dynein transports a wide variety of cargos remains an open question. The FTS-Hook-FHIP ('FHF') cargo adaptor complex links dynein to cargo in humans and fungi. As human cells have three Hooks and four FHIP proteins, we hypothesized that the combinatorial assembly of different Hook and FHIP proteins could underlie dynein cargo diversity. Using proteomic approaches, we determine the protein 'interactome' of each FHIP protein. Live-cell imaging and biochemical approaches show that different FHF complexes associate with distinct motile cargos. These complexes also move with dynein and its cofactor dynactin in single-molecule in vitro reconstitution assays. Complexes composed of FTS, FHIP1B, and Hook1/Hook3 colocalize with Rab5-tagged early endosomes via a direct interaction between FHIP1B and GTP-bound Rab5. In contrast, complexes composed of FTS, FHIP2A, and Hook2 colocalize with Rab1A-tagged ER-to-Golgi cargos and FHIP2A is involved in the motility of Rab1A tubules. Our findings suggest that combinatorial assembly of different FTS-Hook-FHIP complexes is one mechanism dynein uses to achieve cargo specificity.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Cells, Cultured ; Cytoplasmic Dyneins/genetics ; Cytoplasmic Dyneins/metabolism ; Endosomes/genetics ; Endosomes/metabolism ; Humans ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Protein Transport/genetics ; Protein Transport/physiology
Chemical Substances	Adaptor Proteins, Signal Transducing ; Microtubule-Associated Proteins ; Cytoplasmic Dyneins (EC 3.6.4.2)
Language	English
Publishing date	2021-12-09
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.74538
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Article ; Online: Cytoplasmic dynein-1 cargo diversity is mediated by the combinatorial assembly of FTS–Hook–FHIP complexes

Jenna R Christensen / Agnieszka A Kendrick / Joey B Truong / Adriana Aguilar-Maldonado / Vinit Adani / Monika Dzieciatkowska / Samara L Reck-Peterson

eLife, Vol

2021 Volume 10

Abstract	In eukaryotic cells, intracellular components are organized by the microtubule motors cytoplasmic dynein-1 (dynein) and kinesins, which are linked to cargos via adaptor proteins. While ~40 kinesins transport cargo toward the plus end of microtubules, a single dynein moves cargo in the opposite direction. How dynein transports a wide variety of cargos remains an open question. The FTS–Hook–FHIP (‘FHF’) cargo adaptor complex links dynein to cargo in humans and fungi. As human cells have three Hooks and four FHIP proteins, we hypothesized that the combinatorial assembly of different Hook and FHIP proteins could underlie dynein cargo diversity. Using proteomic approaches, we determine the protein ‘interactome’ of each FHIP protein. Live-cell imaging and biochemical approaches show that different FHF complexes associate with distinct motile cargos. These complexes also move with dynein and its cofactor dynactin in single-molecule in vitro reconstitution assays. Complexes composed of FTS, FHIP1B, and Hook1/Hook3 colocalize with Rab5-tagged early endosomes via a direct interaction between FHIP1B and GTP-bound Rab5. In contrast, complexes composed of FTS, FHIP2A, and Hook2 colocalize with Rab1A-tagged ER-to-Golgi cargos and FHIP2A is involved in the motility of Rab1A tubules. Our findings suggest that combinatorial assembly of different FTS–Hook–FHIP complexes is one mechanism dynein uses to achieve cargo specificity.
Keywords	dynein ; dynactin ; endosome ; microtubule ; Rab5 ; Rab1 ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
Subject code	572
Language	English
Publishing date	2021-12-01T00:00:00Z
Publisher	eLife Sciences Publications Ltd
Document type	Article ; Online
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Article ; Online: Streptococcus pneumoniae IgA1 protease: A metalloprotease that can catalyze in a split manner in vitro.

Chi, Ying-Chih / Rahkola, Jeremy T / Kendrick, Agnieszka A / Holliday, Michael J / Paukovich, Natasia / Roberts, Thomas S / Janoff, Edward N / Eisenmesser, Elan Z

Protein science : a publication of the Protein Society

2017 Volume 26, Issue 3, Page(s) 600–610

Abstract: IgA1 proteases (IgA1P) from diverse pathogenic bacteria specifically cleave human immunoglobulin A1 (IgA1) at the hinge region, thereby thwarting protective host immune responses. Streptococcus pneumoniae (S. pneumoniae) IgA1P shares no sequence ... ...

Abstract	IgA1 proteases (IgA1P) from diverse pathogenic bacteria specifically cleave human immunoglobulin A1 (IgA1) at the hinge region, thereby thwarting protective host immune responses. Streptococcus pneumoniae (S. pneumoniae) IgA1P shares no sequence conservation with serine or cysteine types of IgA1Ps or other known proteins, other than a conserved HExxH Zn-binding motif (1604-1608) found in metalloproteases. We have developed a novel expression system to produce the mature S. pneumoniae IgA1P and we have discovered that this form is both attached to the bacterial cell surface and released in its full form. Our data demonstrate that the S. pneumoniae IgA1P comprises two distinct regions that associate to form an active metalloprotease, the first such example of a metalloprotease that can be split in vitro and recombined to form an active enzyme. By capitalizing on this novel domain architecture, we show that the N-terminal region of S. pneumoniae IgA1P comprises the primary binding region for IgA1, although the C-terminal region of S. pneumoniae IgA1P is necessary for cleavage of IgA1. Our findings lend insight into the protein domain architecture of the S. pneumoniae IgA1P and function of this important virulence factor for S. pneumoniae infection.
MeSH term(s)	Amino Acid Motifs ; Bacterial Proteins/chemistry ; Catalysis ; Protein Domains ; Serine Endopeptidases/chemistry ; Streptococcus pneumoniae/enzymology ; Virulence Factors/chemistry
Chemical Substances	Bacterial Proteins ; Virulence Factors ; Serine Endopeptidases (EC 3.4.21.-) ; IgA-specific serine endopeptidase (EC 3.4.21.72)
Language	English
Publishing date	2017-02-23
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	1106283-6
ISSN	1469-896X ; 0961-8368
ISSN (online)	1469-896X
ISSN	0961-8368
DOI	10.1002/pro.3110
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Article ; Online: Hook3 is a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and KIF1C.

Kendrick, Agnieszka A / Dickey, Andrea M / Redwine, William B / Tran, Phuoc Tien / Vaites, Laura Pontano / Dzieciatkowska, Monika / Harper, J Wade / Reck-Peterson, Samara L

The Journal of cell biology

2019 Volume 218, Issue 9, Page(s) 2982–3001

Abstract: The unidirectional and opposite-polarity microtubule-based motors, dynein and kinesin, drive long-distance intracellular cargo transport. Cellular observations suggest that opposite-polarity motors may be coupled. We recently identified an interaction ... ...

Abstract	The unidirectional and opposite-polarity microtubule-based motors, dynein and kinesin, drive long-distance intracellular cargo transport. Cellular observations suggest that opposite-polarity motors may be coupled. We recently identified an interaction between the cytoplasmic dynein-1 activating adaptor Hook3 and the kinesin-3 KIF1C. Here, using in vitro reconstitutions with purified components, we show that KIF1C and dynein/dynactin can exist in a complex scaffolded by Hook3. Full-length Hook3 binds to and activates dynein/dynactin motility. Hook3 also binds to a short region in the "tail" of KIF1C, but unlike dynein/dynactin, this interaction does not activate KIF1C. Hook3 scaffolding allows dynein to transport KIF1C toward the microtubule minus end, and KIF1C to transport dynein toward the microtubule plus end. In cells, KIF1C can recruit Hook3 to the cell periphery, although the cellular role of the complex containing both motors remains unknown. We propose that Hook3's ability to scaffold dynein/dynactin and KIF1C may regulate bidirectional motility, promote motor recycling, or sequester the pool of available dynein/dynactin activating adaptors.
MeSH term(s)	Cell Line, Tumor ; Dyneins/genetics ; Dyneins/metabolism ; Humans ; Kinesins/genetics ; Kinesins/metabolism ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Microtubules/genetics ; Microtubules/metabolism
Chemical Substances	KIF1C protein, human ; Microtubule-Associated Proteins ; hook3 protein, human ; Dyneins (EC 3.6.4.2) ; Kinesins (EC 3.6.4.4)
Language	English
Publishing date	2019-07-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201812170
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Article ; Online: Genomic comparison of two independent seagrass lineages reveals habitat-driven convergent evolution.

Lee, HueyTyng / Golicz, Agnieszka A / Bayer, Philipp E / Severn-Ellis, Anita A / Chan, Chon-Kit Kenneth / Batley, Jacqueline / Kendrick, Gary A / Edwards, David

Journal of experimental botany

2018 Volume 69, Issue 15, Page(s) 3689–3702

Abstract: Seagrasses are marine angiosperms that live fully submerged in the sea. They evolved from land plant ancestors, with multiple species representing at least three independent return-to-the-sea events. This raises the question of whether these marine ... ...

Abstract	Seagrasses are marine angiosperms that live fully submerged in the sea. They evolved from land plant ancestors, with multiple species representing at least three independent return-to-the-sea events. This raises the question of whether these marine angiosperms followed the same adaptation pathway to allow them to live and reproduce under the hostile marine conditions. To compare the basis of marine adaptation between seagrass lineages, we generated genomic data for Halophila ovalis and compared this with recently published genomes for two members of Zosteraceae, as well as genomes of five non-marine plant species (Arabidopsis, Oryza sativa, Phoenix dactylifera, Musa acuminata, and Spirodela polyrhiza). Halophila and Zosteraceae represent two independent seagrass lineages separated by around 30 million years. Genes that were lost or conserved in both lineages were identified. All three species lost genes associated with ethylene and terpenoid biosynthesis, and retained genes related to salinity adaptation, such as those for osmoregulation. In contrast, the loss of the NADH dehydrogenase-like complex is unique to H. ovalis. Through comparison of two independent return-to-the-sea events, this study further describes marine adaptation characteristics common to seagrass families, identifies species-specific gene loss, and provides molecular evidence for convergent evolution in seagrass lineages.
MeSH term(s)	Adaptation, Physiological ; Ecosystem ; Evolution, Molecular ; Genomics ; Hydrocharitaceae/genetics ; Magnoliopsida/genetics ; Species Specificity ; Zosteraceae/genetics
Language	English
Publishing date	2018-06-18
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2976-2
ISSN	1460-2431 ; 0022-0957
ISSN (online)	1460-2431
ISSN	0022-0957
DOI	10.1093/jxb/ery147
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Article: Genomic comparison of two independent seagrass lineages reveals habitat-driven convergent evolution

Lee, HueyTyng / Golicz, Agnieszka A / Bayer, Philipp E / Severn-Ellis, Anita A / Chan, Chon-Kit Kenneth / Batley, Jacqueline / Kendrick, Gary A / Edwards, David

Journal of experimental botany. 2018 June 27, v. 69, no. 15

2018

Abstract	Seagrasses are marine angiosperms that live fully submerged in the sea. They evolved from land plant ancestors, with multiple species representing at least three independent return-to-the-sea events. This raises the question of whether these marine angiosperms followed the same adaptation pathway to allow them to live and reproduce under the hostile marine conditions. To compare the basis of marine adaptation between seagrass lineages, we generated genomic data for Halophila ovalis and compared this with recently published genomes for two members of Zosteraceae, as well as genomes of five non-marine plant species (Arabidopsis, Oryza sativa, Phoenix dactylifera, Musa acuminata, and Spirodela polyrhiza). Halophila and Zosteraceae represent two independent seagrass lineages separated by around 30 million years. Genes that were lost or conserved in both lineages were identified. All three species lost genes associated with ethylene and terpenoid biosynthesis, and retained genes related to salinity adaptation, such as those for osmoregulation. In contrast, the loss of the NADH dehydrogenase-like complex is unique to H. ovalis. Through comparison of two independent return-to-the-sea events, this study further describes marine adaptation characteristics common to seagrass families, identifies species-specific gene loss, and provides molecular evidence for convergent evolution in seagrass lineages.
Keywords	Arabidopsis ; Halophila ; Musa acuminata ; NAD (coenzyme) ; Oryza sativa ; Phoenix dactylifera ; Spirodela polyrhiza ; Zosteraceae ; ancestry ; biosynthesis ; convergent evolution ; ethylene ; gene deletion ; genes ; genomics ; osmoregulation ; salinity ; seagrasses ; terpenoids
Language	English
Dates of publication	2018-0627
Size	p. 3689-3702.
Publishing place	Oxford University Press
Document type	Article
ZDB-ID	2976-2
ISSN	1460-2431 ; 0022-0957
ISSN (online)	1460-2431
ISSN	0022-0957
DOI	10.1093/jxb/ery147
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Article ; Online: CD147: a small molecule transporter ancillary protein at the crossroad of multiple hallmarks of cancer and metabolic reprogramming.

Kendrick, Agnieszka A / Schafer, Johnathon / Dzieciatkowska, Monika / Nemkov, Travis / D'Alessandro, Angelo / Neelakantan, Deepika / Ford, Heide L / Pearson, Chad G / Weekes, Colin D / Hansen, Kirk C / Eisenmesser, Elan Z

Oncotarget

2017 Volume 8, Issue 4, Page(s) 6742–6762

Abstract: Increased expression of CD147 in pancreatic cancer has been proposed to play a critical role in cancer progression via CD147 chaperone function for lactate monocarboxylate transporters (MCTs). Here, we show for the first time that CD147 interacts with ... ...

Abstract	Increased expression of CD147 in pancreatic cancer has been proposed to play a critical role in cancer progression via CD147 chaperone function for lactate monocarboxylate transporters (MCTs). Here, we show for the first time that CD147 interacts with membrane transporters beyond MCTs and exhibits a protective role for several of its interacting partners. CD147 prevents its interacting partner's proteasome-dependent degradation and incorrect plasma membrane localization through the CD147 transmembrane (TM) region. The interactions with transmembrane small molecule and ion transporters identified here indicate a central role of CD147 in pancreatic cancer metabolic reprogramming, particularly with respect to amino acid anabolism and calcium signaling. Importantly, CD147 genetic ablation prevents pancreatic cancer cell proliferation and tumor growth in vitro and in vivo in conjunction with metabolic rewiring towards amino acid anabolism, thus paving the way for future combined pharmacological treatments.
MeSH term(s)	Amino Acids/metabolism ; Animals ; Basigin/genetics ; Basigin/metabolism ; Calcium Signaling ; Cell Adhesion ; Cell Line, Tumor ; Cell Movement ; Cell Proliferation ; Cellular Reprogramming ; Energy Metabolism ; Female ; Gene Expression Regulation, Enzymologic ; Gene Expression Regulation, Neoplastic ; Humans ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Mice, Nude ; Monocarboxylic Acid Transporters/genetics ; Monocarboxylic Acid Transporters/metabolism ; Pancreatic Neoplasms/genetics ; Pancreatic Neoplasms/metabolism ; Pancreatic Neoplasms/pathology ; Plasma Membrane Calcium-Transporting ATPases/genetics ; Plasma Membrane Calcium-Transporting ATPases/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Protein Binding ; Proteolysis ; RNA Interference ; Time Factors ; Transfection ; Tumor Burden
Chemical Substances	ATP2B1 protein, human ; Amino Acids ; BSG protein, human ; Membrane Transport Proteins ; Monocarboxylic Acid Transporters ; Basigin (136894-56-9) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Plasma Membrane Calcium-Transporting ATPases (EC 3.6.3.8)
Language	English
Publishing date	2017-02-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.14272
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