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Article ; Online: Cargo selection in endoplasmic reticulum-to-Golgi transport and relevant diseases.

Tang, Vi T / Ginsburg, David

2023 Volume 133, Issue 1

Abstract: Most proteins destined for the extracellular space or various intracellular compartments must traverse the intracellular secretory pathway. The first step is the recruitment and transport of cargoes from the endoplasmic reticulum (ER) lumen to the Golgi ... ...

Abstract	Most proteins destined for the extracellular space or various intracellular compartments must traverse the intracellular secretory pathway. The first step is the recruitment and transport of cargoes from the endoplasmic reticulum (ER) lumen to the Golgi apparatus by coat protein complex II (COPII), consisting of five core proteins. Additional ER transmembrane proteins that aid cargo recruitment are referred to as cargo receptors. Gene duplication events have resulted in multiple COPII paralogs present in the mammalian genome. Here, we review the functions of each COPII protein, human disorders associated with each paralog, and evidence for functional conservation between paralogs. We also provide a summary of current knowledge regarding two prototypical cargo receptors in mammals, LMAN1 and SURF4, and their roles in human health and disease.
MeSH term(s)	Animals ; Humans ; Protein Transport ; COP-Coated Vesicles/genetics ; COP-Coated Vesicles/metabolism ; Biological Transport/physiology ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/genetics ; Golgi Apparatus/metabolism ; Mammals/metabolism
Chemical Substances	Membrane Proteins ; SURF4 protein, human
Language	English
Publishing date	2023-01-03
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	3067-3
ISSN	1558-8238 ; 0021-9738
ISSN (online)	1558-8238
ISSN	0021-9738
DOI	10.1172/JCI163838
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Article: Nearshore Species Biodiversity of a Marine Protected Area Off Santa Catalina Island, California

Looby, Audrey / Ginsburg, David W

Western North American naturalist. 2021 Mar. 23, v. 81, no. 1

2021

Abstract: Santa Catalina Island, located ∼35 km off the Southern California coast, is home to the Blue Cavern Onshore State Marine Conservation Area (SMCA). Although the conservation area is recognized as both an area of special biological significance and a ... ...

Abstract	Santa Catalina Island, located ∼35 km off the Southern California coast, is home to the Blue Cavern Onshore State Marine Conservation Area (SMCA). Although the conservation area is recognized as both an area of special biological significance and a marine life refuge, species richness of the nearshore taxa from this location is not known. In this study, we provide a comprehensive inventory of the intertidal and subtidal marine macroalgae, plants, invertebrates, and fishes documented from 5 different reef sites inside Blue Cavern Onshore SMCA. Species richness data were compiled using scuba-based visual surveys conducted in the field, references from the primary and gray literature, research collections maintained by scholarly institutions, and field monitoring programs. The total number of marine taxa documented in this study (765 species from 17 major phylogenetic groups) represents 63% of the estimated species richness in Blue Cavern Onshore SMCA and is indicative of the high biodiversity known from this region. Specifically, the intertidal and subtidal biota reported here represent 34% and 18% of the marine taxa known from Catalina Island and the Southern California Bight, respectively. Incidences of the introduction of exotic and invasive organisms (n = 18), changes in the geographic distributions of species (n = 14), as well as marine taxa listed as species of concern, endangered, or critically endangered (n = 4), were also identified in the current inventory. Research findings presented here offer an important baseline of species richness in the California Channel Islands and will help to improve efforts by resource managers and policy makers to conserve and manage similar habitats in the coastal waters off Southern California.
Keywords	caves ; coasts ; inventories ; issues and policy ; littoral zone ; macroalgae ; marine protected areas ; phylogeny ; species richness ; California
Language	English
Dates of publication	2021-0323
Size	p. 113-130.
Publishing place	Brigham Young University
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	2486542-4
ISSN	1944-8341 ; 1527-0904
ISSN (online)	1944-8341
ISSN	1527-0904
DOI	10.3398/064.081.0110
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Introduction of Francis S. Collins.

Ginsburg, David

The Journal of clinical investigation

2015 Volume 125, Issue 9, Page(s) 3321–3327

MeSH term(s)	Genetics, Medical/history ; History, 20th Century ; History, 21st Century ; Humans ; Portraits as Topic
Language	English
Publishing date	2015-09
Publishing country	United States
Document type	Biography ; Historical Article ; Journal Article
ZDB-ID	3067-3
ISSN	1558-8238 ; 0021-9738
ISSN (online)	1558-8238
ISSN	0021-9738
DOI	10.1172/JCI83698
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Article ; Online: The small GTPase RAB10 regulates endosomal recycling of the LDL receptor and transferrin receptor in hepatocytes.

Khan, Taslima Gani / Ginsburg, David / Emmer, Brian T

Journal of lipid research

2022 Volume 63, Issue 8, Page(s) 100248

Abstract: The low-density lipoprotein receptor (LDLR) mediates the hepatic uptake of circulating low-density lipoproteins (LDLs), a process that modulates the development of atherosclerotic cardiovascular disease. We recently identified RAB10, encoding a small ... ...

Abstract	The low-density lipoprotein receptor (LDLR) mediates the hepatic uptake of circulating low-density lipoproteins (LDLs), a process that modulates the development of atherosclerotic cardiovascular disease. We recently identified RAB10, encoding a small GTPase, as a positive regulator of LDL uptake in hepatocellular carcinoma cells (HuH7) in a genome-wide CRISPR screen, though the underlying molecular mechanism for this effect was unknown. We now report that RAB10 regulates hepatocyte LDL uptake by promoting the recycling of endocytosed LDLR from RAB11-positive endosomes to the plasma membrane. We also show that RAB10 similarly promotes the recycling of the transferrin receptor, which binds the transferrin protein that mediates the transport of iron in the blood, albeit from a distinct RAB4-positive compartment. Taken together, our findings suggest a model in which RAB10 regulates LDL and transferrin uptake by promoting both slow and rapid recycling routes for their respective receptor proteins.
MeSH term(s)	Endocytosis ; Endosomes ; Hepatocytes ; Lipoproteins, LDL ; Monomeric GTP-Binding Proteins ; Receptors, LDL ; Receptors, Transferrin ; Transferrin ; rab GTP-Binding Proteins
Chemical Substances	Lipoproteins, LDL ; Receptors, LDL ; Receptors, Transferrin ; Transferrin ; Monomeric GTP-Binding Proteins (EC 3.6.5.2) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2022-06-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80154-9
ISSN	1539-7262 ; 0022-2275
ISSN (online)	1539-7262
ISSN	0022-2275
DOI	10.1016/j.jlr.2022.100248
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Article ; Online: Genome Editing and Hematologic Malignancy.

Emmer, Brian T / Ginsburg, David

Annual review of medicine

2019 Volume 71, Page(s) 71–83

Abstract: The modern genomic era has seen remarkable advancement in our understanding of the molecular basis for disease, yet translation of basic discoveries into new disease treatments has arguably lagged behind. Recently, breakthroughs in genome editing ... ...

Abstract	The modern genomic era has seen remarkable advancement in our understanding of the molecular basis for disease, yet translation of basic discoveries into new disease treatments has arguably lagged behind. Recently, breakthroughs in genome editing technologies have created hope for their potential to directly treat the genetic causes of disease. Like any therapeutic intervention, genome editing should be considered in light of its potential risks and benefits. In this review, we highlight the promise of genome editing therapies, as well as the conceptual and technical barriers to their clinical application, with a special emphasis on hematologic malignancies.
MeSH term(s)	CRISPR-Cas Systems/genetics ; Female ; Gene Editing/methods ; Genetic Therapy/methods ; Hematologic Neoplasms/diagnosis ; Hematologic Neoplasms/genetics ; Hematologic Neoplasms/mortality ; Hematologic Neoplasms/therapy ; Humans ; Male ; Neoplasm Invasiveness/pathology ; Neoplasm Staging ; Prognosis ; Risk Assessment ; Survival Analysis ; Treatment Outcome
Language	English
Publishing date	2019-08-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	207930-6
ISSN	1545-326X ; 0066-4219
ISSN (online)	1545-326X
ISSN	0066-4219
DOI	10.1146/annurev-med-052318-100741
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Article ; Online: Genetics and genomics to the clinic: a long road ahead.

Ginsburg, David

Cell

2011 Volume 147, Issue 1, Page(s) 17–19

Abstract: Advances in genomic technology have produced an explosion of new information about the genetic basis for human disease, fueling extraordinarily high expectations for improved treatments. This perspective will take brief stock of what genetics/genomics ... ...

Abstract	Advances in genomic technology have produced an explosion of new information about the genetic basis for human disease, fueling extraordinarily high expectations for improved treatments. This perspective will take brief stock of what genetics/genomics have brought to clinical practice to date and what we might expect for the future.
MeSH term(s)	Disease/genetics ; Genome-Wide Association Study ; Genomics ; Humans ; Male ; Mutation
Language	English
Publishing date	2011-09-29
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2011.09.013
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Zs.MG 58: Show issues

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Article ; Online: Identification of LMAN1- and SURF4-Dependent Secretory Cargoes.

Tang, Vi T / Abbineni, Prabhodh S / Veiga Leprevost, Felipe da / Basrur, Venkatesha / Khoriaty, Rami / Emmer, Brian T / Nesvizhskii, Alexey I / Ginsburg, David

Journal of proteome research

2023 Volume 22, Issue 11, Page(s) 3439–3446

Abstract: Most proteins secreted into the extracellular space are first recruited from the endoplasmic reticulum into coat protein complex II (COPII)-coated vesicles or tubules that facilitate their transport to the Golgi apparatus. Although several secreted ... ...

Abstract	Most proteins secreted into the extracellular space are first recruited from the endoplasmic reticulum into coat protein complex II (COPII)-coated vesicles or tubules that facilitate their transport to the Golgi apparatus. Although several secreted proteins have been shown to be actively recruited into COPII vesicles and tubules by the cargo receptors LMAN1 and SURF4, the full cargo repertoire of these receptors is unknown. We now report mass spectrometry analysis of conditioned media and cell lysates from HuH7 cells CRISPR targeted to inactivate the
MeSH term(s)	Humans ; Carrier Proteins/metabolism ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus ; Membrane Proteins/metabolism ; Protein Transport
Chemical Substances	Carrier Proteins ; Membrane Proteins ; SURF4 protein, human
Language	English
Publishing date	2023-10-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021/acs.jproteome.3c00259
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Article: Identification of LMAN1 and SURF4 dependent secretory cargoes.

Tang, Vi T / Abbineni, Prabhodh S / Leprevost, Felipe da Veiga / Basrur, Venkatesha / Emmer, Brian T / Nesvizhskii, Alexey I / Ginsburg, David

bioRxiv : the preprint server for biology

2023

Abstract	Most proteins secreted into the extracellular space are first recruited from the endoplasmic reticulum into coat protein complex II (COPII)-coated vesicles or tubules that facilitate their transport to the Golgi apparatus. Although several secreted proteins have been shown to be actively recruited into COPII vesicles/tubules by the cargo receptors LMAN1 and SURF4, the full cargo repertoire of these receptors is unknown. We now report mass spectrometry analysis of conditioned media and cell lysates from HuH7 cells CRISPR targeted to inactivate the
Language	English
Publishing date	2023-04-06
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.04.06.535922
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Article: Functional overlap between the mammalian

Tang, Vi T / Xiang, Jie / Chen, Zhimin / McCormick, Joseph / Abbineni, Prabhodh S / Chen, Xiao-Wei / Hoenerhoff, Mark / Emmer, Brian T / Khoriaty, Rami / Lin, Jiandie D / Ginsburg, David

bioRxiv : the preprint server for biology

2024

Abstract: Proteins carrying a signal peptide and/or a transmembrane domain enter the intracellular secretory pathway at the endoplasmic reticulum (ER) and are transported to the Golgi apparatus via COPII vesicles or tubules. SAR1 initiates COPII coat assembly by ... ...

Abstract	Proteins carrying a signal peptide and/or a transmembrane domain enter the intracellular secretory pathway at the endoplasmic reticulum (ER) and are transported to the Golgi apparatus via COPII vesicles or tubules. SAR1 initiates COPII coat assembly by recruiting other coat proteins to the ER membrane. Mammalian genomes encode two
Language	English
Publishing date	2024-02-29
Publishing country	United States
Document type	Preprint
DOI	10.1101/2024.02.27.582310
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Article ; Online: Altered phenotype in LMAN1-deficient mice with low levels of residual LMAN1 expression.

Everett, Lesley A / Khoriaty, Rami N / Zhang, Bin / Ginsburg, David

Blood advances

2020 Volume 4, Issue 22, Page(s) 5635–5643

Abstract: Combined deficiency of coagulation factors V and VIII (F5F8D) is an autosomal recessive bleeding disorder caused by loss-of-function mutations in either LMAN1 or MCFD2. The latter genes encode 2 components of a mammalian cargo receptor that facilitates ... ...

Abstract	Combined deficiency of coagulation factors V and VIII (F5F8D) is an autosomal recessive bleeding disorder caused by loss-of-function mutations in either LMAN1 or MCFD2. The latter genes encode 2 components of a mammalian cargo receptor that facilitates secretion of coagulation factor V (FV) and factor VIII (FVIII) from the endoplasmic reticulum (ER) to the Golgi via coat protein complex II vesicles. F5F8D patients exhibit FV and FVIII levels that are ∼10% to 15% of normal. We report herein a comparative analysis for a series of murine Lman1 alleles. Consistent with previous reports, mice completely deficient in LMAN1 (Lman1-/-) exhibit ∼50% FV and FVIII levels. In contrast, mice carrying a hypomorphic Lman1 allele (Lman1cgt/cgt) that expresses ∼6% to 8% of wild-type Lman1 mRNA levels exhibit intermediate plasma FV and FVIII reductions (∼70% of wild-type levels). Lman1-/- mice exhibit ER accumulation of another LMAN1 cargo, alpha-1 antitrypsin (A1AT), with an intermediate level of A1AT ER retention observed in Lman1cgt/cgt mice. Finally, the previously reported strain-specific, partially penetrant, perinatal lethality of LMAN1-deficient mice (Lman1gt1/gt1) was confirmed in Lman1-/- mice, although it was not observed in Lman1cgt/cgt mice. Taken together, these results show a dose-dependent effect of residual LMAN1 on the secretion of its cargo proteins. The results also suggest that human subjects with hypomorphic LMAN1 mutations might present with mild bleeding phenotypes resulting from more modest reductions in FV and FVIII, which could be missed by routine clinical evaluation. Finally, these findings suggest that therapeutic targeting of LMAN1 to reduce FV and FVIII as an anticoagulant strategy may only require partial inhibition of LMAN1 function.
MeSH term(s)	Animals ; Calcium-Binding Proteins ; Factor V Deficiency/genetics ; Mannose-Binding Lectins/genetics ; Membrane Proteins/genetics ; Mice ; Phenotype
Chemical Substances	Calcium-Binding Proteins ; ERGIC-53 protein, mouse ; Mannose-Binding Lectins ; Membrane Proteins
Language	English
Publishing date	2020-10-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2915908-8
ISSN	2473-9537 ; 2473-9529
ISSN (online)	2473-9537
ISSN	2473-9529
DOI	10.1182/bloodadvances.2020002523
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