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Article ; Online: ER-to-Golgi Transport: A Sizeable Problem.

McCaughey, Janine / Stephens, David J

2019 Volume 29, Issue 12, Page(s) 940–953

Abstract: Metazoans require efficient and ordered secretion of extracellular matrix (ECM) to coordinate cell and tissue function. Many ECM proteins are atypically large and their demand during key stages of development presents a major challenge to the canonical ... ...

Abstract	Metazoans require efficient and ordered secretion of extracellular matrix (ECM) to coordinate cell and tissue function. Many ECM proteins are atypically large and their demand during key stages of development presents a major challenge to the canonical secretion machinery. While many of the molecular players in this pathway are known, little is understood about how they are integrated in time and space. Recent advances in gene engineering and super-resolution microscopy have underscored the spatiotemporal organisation of the endoplasmic reticulum (ER)-Golgi interface. These findings are challenging long-held models of vesicular transport of large matrix proteins, such as procollagen, and are implicating less well-defined carriers and direct interconnections between organelles. Here, we discuss current models describing the dynamics and mechanisms of ER-Golgi transport.
MeSH term(s)	Animals ; COP-Coated Vesicles/metabolism ; Endoplasmic Reticulum/metabolism ; Extracellular Matrix/metabolism ; Extracellular Matrix Proteins/metabolism ; Golgi Apparatus/metabolism ; Humans ; Protein Transport/physiology ; Vesicular Transport Proteins/metabolism
Chemical Substances	Extracellular Matrix Proteins ; Vesicular Transport Proteins
Language	English
Publishing date	2019-10-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	30122-x
ISSN	1879-3088 ; 0962-8924
ISSN (online)	1879-3088
ISSN	0962-8924
DOI	10.1016/j.tcb.2019.08.007
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Article ; Online: COPII-dependent ER export in animal cells: adaptation and control for diverse cargo.

McCaughey, Janine / Stephens, David J

Histochemistry and cell biology

2018 Volume 150, Issue 2, Page(s) 119–131

Abstract: The export of newly synthesized proteins from the endoplasmic reticulum is fundamental to the ongoing maintenance of cell and tissue structure and function. After co-translational translocation into the ER, proteins destined for downstream intracellular ... ...

Abstract	The export of newly synthesized proteins from the endoplasmic reticulum is fundamental to the ongoing maintenance of cell and tissue structure and function. After co-translational translocation into the ER, proteins destined for downstream intracellular compartments or secretion from the cell are sorted and packaged into transport vesicles by the COPII coat protein complex. The fundamental discovery and characterization of the pathway has now been augmented by a greater understanding of the role of COPII in diverse aspects of cell function. We now have a deep understanding of how COPII contributes to the trafficking of diverse cargoes including extracellular matrix molecules, developmental signalling proteins, and key metabolic factors such as lipoproteins. Structural and functional studies have shown that the COPII coat is both highly flexible and subject to multiple modes of regulation. This has led to new discoveries defining roles of COPII in development, autophagy, and tissue organization. Many of these newly emerging features of the canonical COPII pathway are placed in a context of procollagen secretion because of the fundamental interest in how a coat complex that typically generates 80-nm transport vesicles can package a cargo reported to be over 300 nm. Here we review the current understanding of COPII and assess the current consensus on its role in packaging diverse cargo proteins.
MeSH term(s)	Animals ; COP-Coated Vesicles/metabolism ; Endoplasmic Reticulum/metabolism ; Protein Transport ; Proteins/metabolism
Chemical Substances	Proteins
Language	English
Publishing date	2018-06-18
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	1222930-1
ISSN	1432-119X ; 0301-5564 ; 0948-6143
ISSN (online)	1432-119X
ISSN	0301-5564 ; 0948-6143
DOI	10.1007/s00418-018-1689-2
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Article ; Online: ER-to-Golgi trafficking of procollagen in the absence of large carriers.

McCaughey, Janine / Stevenson, Nicola L / Cross, Stephen / Stephens, David J

The Journal of cell biology

2018 Volume 218, Issue 3, Page(s) 929–948

Abstract: Secretion and assembly of collagen are fundamental to the function of the extracellular matrix. Defects in the assembly of a collagen matrix lead to pathologies including fibrosis and osteogenesis imperfecta. Owing to the size of fibril-forming ... ...

Abstract	Secretion and assembly of collagen are fundamental to the function of the extracellular matrix. Defects in the assembly of a collagen matrix lead to pathologies including fibrosis and osteogenesis imperfecta. Owing to the size of fibril-forming procollagen molecules it is assumed that they are transported from the endoplasmic reticulum to the Golgi in specialized large COPII-dependent carriers. Here, analyzing endogenous procollagen and a new engineered GFP-tagged form, we show that transport to the Golgi occurs in the absence of large (>350 nm) carriers. Large GFP-positive structures were observed occasionally, but these were nondynamic, are not COPII positive, and are labeled with markers of the ER. We propose a short-loop model of COPII-dependent ER-to-Golgi traffic that, while consistent with models of ERGIC-dependent expansion of COPII carriers, does not invoke long-range trafficking of large vesicular structures. Our findings provide an important insight into the process of procollagen trafficking and reveal a short-loop pathway from the ER to the Golgi, without the use of large carriers.
MeSH term(s)	Biological Transport, Active/physiology ; COP-Coated Vesicles/metabolism ; Cell Line, Transformed ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/metabolism ; Humans ; Models, Biological
Language	English
Publishing date	2018-12-26
Publishing country	United States
Document type	Journal Article ; 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.201806035
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Article ; Online: A general role for TANGO1, encoded by MIA3, in secretory pathway organization and function.

McCaughey, Janine / Stevenson, Nicola L / Mantell, Judith M / Neal, Chris R / Paterson, Alex / Heesom, Kate / Stephens, David J

Journal of cell science

2021 Volume 134, Issue 17

Abstract: Complex machinery is required to drive secretory cargo export from the endoplasmic reticulum (ER), which is an essential process in eukaryotic cells. In vertebrates, the MIA3 gene encodes two major forms of transport and Golgi organization protein 1 ( ... ...

Abstract	Complex machinery is required to drive secretory cargo export from the endoplasmic reticulum (ER), which is an essential process in eukaryotic cells. In vertebrates, the MIA3 gene encodes two major forms of transport and Golgi organization protein 1 (TANGO1S and TANGO1L), which have previously been implicated in selective trafficking of procollagen. Using genome engineering of human cells, light microscopy, secretion assays, genomics and proteomics, we show that disruption of the longer form, TANGO1L, results in relatively minor defects in secretory pathway organization and function, including having limited impacts on procollagen secretion. In contrast, loss of both long and short forms results in major defects in cell organization and secretion. These include a failure to maintain the localization of ERGIC53 (also known as LMAN1) and SURF4 to the ER-Golgi intermediate compartment and dramatic changes to the ultrastructure of the ER-Golgi interface. Disruption of TANGO1 causes significant changes in early secretory pathway gene and protein expression, and impairs secretion not only of large proteins, but of all types of secretory cargo, including small soluble proteins. Our data support a general role for MIA3/TANGO1 in maintaining secretory pathway structure and function in vertebrate cells.
MeSH term(s)	Animals ; Aryl Hydrocarbon Receptor Nuclear Translocator/metabolism ; COP-Coated Vesicles/genetics ; COP-Coated Vesicles/metabolism ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/genetics ; Golgi Apparatus/metabolism ; Humans ; Membrane Proteins/metabolism ; Protein Transport ; Secretory Pathway
Chemical Substances	Membrane Proteins ; SURF4 protein, human ; Aryl Hydrocarbon Receptor Nuclear Translocator (138391-32-9)
Language	English
Publishing date	2021-09-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.259075
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Article ; Online: Developing pathways to clarify pathogenicity of unclassified variants in Osteogenesis Imperfecta genetic analysis.

Balasubramanian, Meena / Hobson, Emma / Skae, Mars / McCaughey, Janine / Stephens, David J

Molecular genetics & genomic medicine

2019 Volume 7, Issue 12, Page(s) e912

Abstract: Background: With increased access to genetic testing, variants of uncertain significance (VUS) where pathogenicity is uncertain are being increasingly identified. More than 85% Osteogenesis Imperfecta (OI) patients have pathogenic variants in COL1A1/A2. ...

Abstract	Background: With increased access to genetic testing, variants of uncertain significance (VUS) where pathogenicity is uncertain are being increasingly identified. More than 85% Osteogenesis Imperfecta (OI) patients have pathogenic variants in COL1A1/A2. However, when a VUS is identified, there are no pathways in place for determining significance. Objective: Define a diagnostic pathway to confirm pathogenicity, providing patients with definitive genetic diagnosis, accurate recurrence risks, and prenatal testing options. Methods: Functional studies on collagen secretion from cultured patient fibroblasts combined with detailed phenotyping and segregation family studies. Results: We demonstrate data from a family with a VUS identified in type I collagen. FAMILY-1: Six-year-old boy with failure-to-gain weight, talipes, fractures, on and off treatment with Pamidronate as diagnosis of OI uncertain. Transiliac bone biopsy at 2 years of age demonstrated active new bone formation within periosteum; bone cortices were normal thickness but increased porosity. Trabecular bone showed features of advanced osteoporosis. Genetic testing identified a de novo COL1A1 c.206_208delTGT, p.Leu69del variant. Sibling with similar phenotype but no fractures as yet, tested positive for variant raising concerns regarding her diagnosis, and management. Results from three independent experiments (cell immunofluorescence, collagen secretion assay by Western Blot, and unbiased proteomics) from cultured patient fibroblasts demonstrate COL1A1 c.206_208delTGT, p.Leu69del variant causing a substantial defect to collagen extracellular matrix assembly confirming variant pathogenicity. Conclusion: Access to genetic testing in OI is increasing as advances in genetic technologies decreases cost; a clinical diagnostic pathway needs to be implemented for managing variants identified by such testing.
MeSH term(s)	Adult ; Child ; Child, Preschool ; Collagen Type I/genetics ; Collagen Type I/metabolism ; Family ; Female ; Fibroblasts ; Fractures, Bone/genetics ; Genetic Testing/ethics ; Genetic Testing/methods ; Genetic Variation ; Humans ; Incidental Findings ; Infant ; Male ; Mutation ; Osteogenesis Imperfecta/genetics ; Osteogenesis Imperfecta/pathology ; Phenotype ; Primary Cell Culture ; Virulence
Chemical Substances	COL1A2 protein, human ; Collagen Type I ; collagen type I, alpha 1 chain
Language	English
Publishing date	2019-09-30
Publishing country	United States
Document type	Case Reports ; Journal Article
ZDB-ID	2734884-2
ISSN	2324-9269 ; 2324-9269
ISSN (online)	2324-9269
ISSN	2324-9269
DOI	10.1002/mgg3.912
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Article ; Online: Perioperative management for people with kidney failure receiving dialysis: A scoping review.

Harrison, Tyrone G / Hemmelgarn, Brenda R / Farragher, Janine F / O'Rielly, Connor / Donald, Maoliosa / James, Matthew T / McCaughey, Deirdre / Ruzycki, Shannon M / Zarnke, Kelly B / Ronksley, Paul E

Seminars in dialysis

2022 Volume 36, Issue 1, Page(s) 57–66

Abstract: Background: People with kidney failure receiving dialysis (CKD-G5D) are more likely to undergo surgery and experience poorer postoperative outcomes than those without kidney failure. In this scoping review, we aimed to systematically identify and ... ...

Abstract	Background: People with kidney failure receiving dialysis (CKD-G5D) are more likely to undergo surgery and experience poorer postoperative outcomes than those without kidney failure. In this scoping review, we aimed to systematically identify and summarize perioperative strategies, protocols, pathways, and interventions that have been studied or implemented for people with CKD-G5D. Methods: We searched MEDLINE, EMBASE, CINAHL Plus, Cochrane Database of Systematic Reviews, and Cochrane Controlled Trials registry (inception to February 2020), in addition to an extensive grey literature search, for sources that reported on a perioperative strategy to guide management for people with CKD-G5D. We summarized the overall study characteristics and perioperative management strategies and identified evidence gaps based on surgery type and perioperative domain. Publication trends over time were assessed, stratified by surgery type and study design. Results: We included 183 studies; the most common study design was a randomized controlled trial (27%), with 67% of publications focused on either kidney transplantation or dialysis vascular access. Transplant-related studies often focused on fluid and volume management strategies and risk stratification, whereas dialysis vascular access studies focused most often on imaging. The number of publications increased over time, across all surgery types, though driven by non-randomized study designs. Conclusions: Despite many current gaps in perioperative research for patients with CKD-G5D, evidence generation supporting perioperative management is increasing, with recent growth driven primarily by non-randomized studies. Our review may inform organization of evidence-based strategies into perioperative care pathways where evidence is available while also highlighting gaps that future perioperative research can address.
MeSH term(s)	Humans ; Renal Dialysis ; Systematic Reviews as Topic ; Perioperative Care/methods ; Renal Insufficiency, Chronic/complications ; Renal Insufficiency, Chronic/therapy ; Renal Insufficiency ; Randomized Controlled Trials as Topic
Language	English
Publishing date	2022-04-05
Publishing country	United States
Document type	Review ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1028193-9
ISSN	1525-139X ; 0894-0959
ISSN (online)	1525-139X
ISSN	0894-0959
DOI	10.1111/sdi.13081
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Article ; Online: Perioperative management for people with chronic kidney disease receiving dialysis undergoing major surgery

Paul E Ronksley / Matthew James / Janine F Farragher / Brenda R Hemmelgarn / Shannon M Ruzycki / Maoliosa Donald / Tyrone G Harrison / Connor O'Rielly / Deirdre McCaughey / Kelly B Zarnke

BMJ Open, Vol 10, Iss

a protocol for a scoping review

2020 Volume 9

Keywords	Medicine ; R
Language	English
Publishing date	2020-09-01T00:00:00Z
Publisher	BMJ Publishing Group
Document type	Article ; Online
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Article ; Online: Perioperative management for people with chronic kidney disease receiving dialysis undergoing major surgery: a protocol for a scoping review.

Harrison, Tyrone G / Hemmelgarn, Brenda R / Farragher, Janine F / O'Rielly, Connor / Donald, Maoliosa / James, Matthew / McCaughey, Deirdre / Ruzycki, Shannon M / Zarnke, Kelly B / Ronksley, Paul E

BMJ open

2020 Volume 10, Issue 9, Page(s) e038725

Abstract: Introduction: People with chronic kidney disease receiving dialysis (CKD G5D) have an increased risk of poor postoperative outcomes and a high incidence of major surgery. Despite the high burden of these combined risks, there is a paucity of evidence to ...

Abstract	Introduction: People with chronic kidney disease receiving dialysis (CKD G5D) have an increased risk of poor postoperative outcomes and a high incidence of major surgery. Despite the high burden of these combined risks, there is a paucity of evidence to support tailored perioperative strategies to manage this population. A comprehensive evidence synthesis would inform the management of these patients in the perioperative period and identify knowledge gaps. We describe a protocol for a scoping review of the literature to identify existing perioperative strategies, protocols, pathways and interventions for people with CKD G5D undergoing major surgery. Methods and analysis: We will conduct a scoping review in accordance with the Joanna Briggs Institute methodology and report per the Preferred Reporting Items for Systematic Reviews and Meta-Analyses extension for scoping reviews. In February 2020, we will complete our search of MEDLINE, EMBASE, CINAHL Plus, Cochrane Database of Systematic Reviews, and Cochrane Controlled Trials Registry for published literature from inception to present. All study types are eligible for inclusion, without language restriction. Studies reporting a perioperative intervention in adult patients with CKD G5D are eligible for inclusion. Studies in prevalent kidney transplant patients or patients with acute kidney injury, and studies that report on surgical approaches without consideration of perioperative management strategies, will be excluded. Reviewers will independently assess abstracts for all identified studies in duplicate, and again at the full-text stage. Following published literature searches, a search of the grey literature will be developed. We will extract and narratively report study, participant and intervention details. This will include a summary table outlining the strategies employed, organised into post hoc developed perioperative domains. Ethics and dissemination: Ethical considerations do not apply to this scoping review. Findings will be disseminated through relevant conference presentations and publications.
MeSH term(s)	Adult ; Humans ; Kidney Transplantation ; Renal Dialysis ; Renal Insufficiency, Chronic/complications ; Renal Insufficiency, Chronic/therapy ; Research Design ; Review Literature as Topic ; Systematic Reviews as Topic
Keywords	covid19
Language	English
Publishing date	2020-09-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2599832-8
ISSN	2044-6055 ; 2044-6055
ISSN (online)	2044-6055
ISSN	2044-6055
DOI	10.1136/bmjopen-2020-038725
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Article ; Online: TFG Promotes Organization of Transitional ER and Efficient Collagen Secretion.

McCaughey, Janine / Miller, Victoria J / Stevenson, Nicola L / Brown, Anna K / Budnik, Annika / Heesom, Kate J / Alibhai, Dominic / Stephens, David J

Cell reports

2016 Volume 15, Issue 8, Page(s) 1648–1659

Abstract: Collagen is the most abundant protein in the animal kingdom. It is of fundamental importance during development for cell differentiation and tissue morphogenesis as well as in pathological processes such as fibrosis and cancer cell migration. However, ... ...

Abstract	Collagen is the most abundant protein in the animal kingdom. It is of fundamental importance during development for cell differentiation and tissue morphogenesis as well as in pathological processes such as fibrosis and cancer cell migration. However, our understanding of the mechanisms of procollagen secretion remains limited. Here, we show that TFG organizes transitional ER (tER) and ER exit sites (ERESs) into larger structures. Depletion of TFG results in dispersion of tER elements that remain associated with individual ER-Golgi intermediate compartments (ERGICs) as largely functional ERESs. We show that TFG is not required for the transport and packaging of small soluble cargoes but is necessary for the export of procollagen from the ER. Our work therefore suggests a key relationship between the structure and function of ERESs and a central role for TFG in optimizing COPII assembly for procollagen export.
MeSH term(s)	Collagen/metabolism ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/metabolism ; Green Fluorescent Proteins/metabolism ; Humans ; Mannosidases/metabolism ; Models, Biological ; Protein Transport ; Proteins/metabolism ; RNA, Small Interfering/metabolism ; Reproducibility of Results
Chemical Substances	Proteins ; RNA, Small Interfering ; TFG protein, human ; Green Fluorescent Proteins (147336-22-9) ; Collagen (9007-34-5) ; Mannosidases (EC 3.2.1.-) ; mannosyl-oligosaccharide 1,3 - 1,6-alpha-mannosidase (EC 3.2.1.114)
Language	English
Publishing date	2016-05-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2016.04.062
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Article ; Online: Regulator of calcineurin-2 is a centriolar protein with a role in cilia length control.

Stevenson, Nicola L / Bergen, Dylan J M / Xu, Amadeus / Wyatt, Emily / Henry, Freya / McCaughey, Janine / Vuolo, Laura / Hammond, Chrissy L / Stephens, David J

Journal of cell science

2018 Volume 131, Issue 9

Abstract: Almost every cell in the human body extends a primary cilium. Defective cilia function leads to a set of disorders known as ciliopathies, which are characterised by debilitating developmental defects that affect many tissues. Here, we report a new role ... ...

Abstract	Almost every cell in the human body extends a primary cilium. Defective cilia function leads to a set of disorders known as ciliopathies, which are characterised by debilitating developmental defects that affect many tissues. Here, we report a new role for regulator of calcineurin 2 (RCAN2) in primary cilia function. It localises to centrioles and the basal body and is required to maintain normal cilia length. RCAN2 was identified as the most strongly upregulated gene from a comparative RNAseq analysis of cells in which expression of the Golgi matrix protein giantin had been abolished by gene editing. In contrast to previous work where we showed that depletion of giantin by RNAi results in defects in ciliogenesis and in cilia length control, giantin knockout cells generate normal cilia after serum withdrawal. Furthermore, giantin knockout zebrafish show increased expression of RCAN2. Importantly, suppression of RCAN2 expression in giantin knockout cells results in the same defects in the control of cilia length that are seen upon RNAi of giantin itself. Together, these data define RCAN2 as a regulator of cilia function that can compensate for the loss of giantin function.
MeSH term(s)	Animals ; Cell Cycle Proteins/metabolism ; Centrioles/genetics ; Centrioles/metabolism ; Cilia/genetics ; Cilia/metabolism ; Gene Knockout Techniques ; Golgi Matrix Proteins/genetics ; Golgi Matrix Proteins/metabolism ; Humans ; Muscle Proteins/genetics ; Muscle Proteins/metabolism ; Retinal Pigment Epithelium/cytology ; Retinal Pigment Epithelium/metabolism ; Zebrafish
Chemical Substances	Cell Cycle Proteins ; Golgi Matrix Proteins ; Muscle Proteins ; RCAN2 protein, human ; macrogolgin
Language	English
Publishing date	2018-05-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.212258
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