ArticleThe Journal of cell biology1981
Studies on the motility of the foraminifera. I. Ultrastructure of the reticulopodial network of Allogromia laticollaris (Arnold).
Article in The Journal of cell biology, 1981. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 94 citations in OpenAlex.
- Single Cell Transcriptomics, Mega-Phylogeny, and the Genetic Basis of Morphological Innovations in Rhizaria.Molecular biology and evolution · 2017Article
- Cytological Observations of the Large Symbiotic Foraminifer Amphisorus kudakajimensis Using Calcein Acetoxymethyl Ester.PloS one · 2016Article
- Genome dynamics are influenced by food source in Allogromia laticollaris strain CSH (Foraminifera).Genome biology and evolution · 2010Article
- Dynamic shape changes of cytoplasmic organelles translocating along microtubules.The Journal of cell biology · 1987Article
- Analysis of the spatial organization of microtubule-associated proteins.The Journal of cell biology · 1986Article
- The structure of cytoplasm in directly frozen cultured cells. II. Cytoplasmic domains associated with organelle movements.The Journal of cell biology · 1986Article
- Bidirectional organelle transport can occur in cell processes that contain single microtubules.The Journal of cell biology · 1985Article
- Detection of single microtubules in living cells: particle transport can occur in both directions along the same microtubule.The Journal of cell biology · 1984Article
- Bidirectional transport of fluorescently labeled vesicles introduced into extruded axoplasm of squid Loligo pealei.The Journal of cell biology · 1984Article
- Studies on the motility of the foraminifera. II. The dynamic microtubular cytoskeleton of the reticulopodial network of Allogromia laticollaris.The Journal of cell biology · 1983Article
- Firm structural associations between migratory pigment granules and microtubules in crayfish retinula cells.The Journal of cell biology · 1983Article
- Association between endocrine pancreatic secretory granules and in-vitro-assembled microtubules is dependent upon microtubule-associated proteins.The Journal of cell biology · 1982Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Allogromia laticollaris, a benthic marine foraminifer, extends numerous trunk filopodia that repeatedly branch, anastomose, and fuse again to form the reticulopodial network (RPN), within which an incessant streaming of cytoplasmic particles occurs. The motion of the particles is saltatory and bidirectional, even in the thinnest filopodia detected by optical microscopy. Fibrils are visible by differential interference microscopy, and the PRN displays positive birefringence in polarized light. These fibrils remain intact after lysis and extraction of the RPN in solutions that stabilize microtubules (MTs). Electron micrographs of thin sections through these lysed and stabilized cytoskeletal models reveal bundles of MTs. The RPNs of living Allogromia may be preserved by standard EM fixatives only after acclimatization to calcium-free seawater, in which the streaming is normal. The MTs in the RPN are typically arranged in bundles that generally lie parallel to the long axis of the trunk and branch filopodia. Stereo electron micrographs of whole-mount, fixed, and critical-point-dried organisms show that the complex pattern of MT deployment reflects the pattern of particle motion in both flattened and highly branched portions of the RPN. Cytoplasmic particles, some of which have a fuzzy coat, are closely associated with, and preferentially oriented along, either single MTs or MT bundles. Thin filaments (approximately 5 nm) are also observed within the network, lying parallel to and interdigitating with the MTs, and in flattened terminal areas of the filopodia. These filaments do not bind skeletal muscle myosin S1 under conditions that heavily decorate actin filaments in controls (human blood platelets), and are approximately 20% too thin to be identified ultrastructurally as F-actin.
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