WordNet

a long thin implement made of metal or wood
any rod-shaped bacterium
a visual receptor cell that is sensitive to dim light (同)rod_cell, retinal rod
the commonest protein in muscle; a globulin that combines with actin to form actomyosin

PrepTutorEJDIC

(木製・金属製などの)『棒,つえ』,さお;釣りざお / (刑罰に用いる)木のむち;《the ~》むち打ち,せっかん / ロッド(長さの単位;『5』1/2yards,約5m) / (目の)桿(かん)状体(弱い光にも感じる網膜細胞) / 《米俗》ピストル
roentgen / recto

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Distinct localizations and roles of non-muscle myosin II during proplatelet formation and platelet release.

Badirou I1, Pan J, Souquere S, Legrand C, Pierron G, Wang A, Eckly A, Roy A, Gachet C, Vainchenker W, Chang Y, Léon C.
Journal of thrombosis and haemostasis : JTH.J Thromb Haemost.2015 May;13(5):851-9. doi: 10.1111/jth.12887. Epub 2015 Apr 1.
BACKGROUND: At the end of maturation, megakaryocytes (MKs) form long cytoplasmic extensions called proplatelets (PPT). Enormous changes in cytoskeletal structures cause PPT to extend further, to re-localize organelles such as mitochondria and to fragment, leading to platelet release. Two non-muscle
PMID 25736522

Flightless I interacts with NMMIIA to promote cell extension formation that enables collagen remodeling.

Arora PD1, Wang Y1, Bresnick A2, Janmey PA3, McCulloch CA4.
Molecular biology of the cell.Mol Biol Cell.2015 Apr 15. pii: mbc.E14-11-1536. [Epub ahead of print]
We examined the role of actin capping protein flightlessI (FliI) in collagen remodeling by mouse fibroblasts. FliI overexpressing cells exhibited reduced spreading on collagen but formed elongated protrusions, which stained for myosin10 and fascin, and penetrated pores of collagen-coated membranes.
PMID 25877872

Aberrant post-translational modifications compromise human myosin motor function in old age.

Li M1, Ogilvie H, Ochala J, Artemenko K, Iwamoto H, Yagi N, Bergquist J, Larsson L.
Aging cell.Aging Cell.2015 Apr;14(2):228-35. doi: 10.1111/acel.12307. Epub 2015 Feb 2.
Novel experimental methods, including a modified single fiber in vitro motility assay, X-ray diffraction experiments, and mass spectrometry analyses, have been performed to unravel the molecular events underlying the aging-related impairment in human skeletal muscle function at the motor protein lev
PMID 25645586

Satoh Aiko,Kinoshita Yasunori,Konno Kunihiko
Fisheries Science 79(2), 341-347, 2013-03
… Monomeric myosin and salt-solubility one decreased much faster than Ca2+-ATPase inactivation in both Ca-, and EDTA-media, which was well explained by the faster rod denaturation than subfragment-1 (S-1) denaturation. … In contrast, when myofibrils were heated at 0.5 M KCl, slow decrease of salt solubility was characteristic, which was also explained by a slow denaturation of rod portion of myosin. …
NAID 120005228080

Investigation on Structural Changes of Myofibrillar Proteins from Silver Carp (Hypophthalmichthys molitrix) during Frozen Storage

LINA Ren,YANSHUN Xu,QIXING Jiang,WENSHUI Xia,CHUNJIANG Qiu
Food Science and Technology Research 19(6), 1051-1059, 2013
… Differential scanning calorimetry thermograms demonstrated that the thermal stability of MP decreased and some structural changes occurred particularly in the rod-like tail portion of myosin. …
NAID 130003392397

Thermal denaturation profiles of catfish and tilapia myofibrils as affected by pH for heating

Thavaroj Wichulada,Pansawat Nantipa,Konno Kunihiko
Fisheries science : FS 78(2), 431-439, 2012-03-01
… Thermal denaturation profiles of catfish myosin when heated as myofibrils (Mf) were compared with those of tilapia ones. … The conclusion was the same with isolated myosin. … Catfish Mf was clearly distinguished form tilapia Mf in subfragment-1 (S-1) and rod denaturation. … A quick denaturation of rod relative to S-1 was characteristic for catfish Mf while a slower denaturation of rod relative to S-1 was the pattern of tilapia Mf. …
NAID 10030125071