메뉴 건너뛰기




Volumn 49, Issue 1, 2009, Pages 79-89

Molecular mechanics of stutter defects in vimentin intermediate filaments

Author keywords

Alpha helix; Coiled coil; Cytoskeleton; Defect; Elasticity; Fracture; Hydrogen bond; Intermediate filaments; Mechanics; Persistence length; Protein; Vimentin

Indexed keywords

ALPHA-HELIX; COILED-COIL; CYTOSKELETON; DEFECT; FRACTURE; HYDROGEN BOND; INTERMEDIATE FILAMENTS; PERSISTENCE LENGTH; PROTEIN; VIMENTIN;

EID: 58949097134     PISSN: 00144851     EISSN: 17412765     Source Type: Journal    
DOI: 10.1007/s11340-007-9100-6     Document Type: Article
Times cited : (12)

References (39)
  • 2
    • 4344685822 scopus 로고    scopus 로고
    • Scaffolds, levers, rods and springs: Diverse cellular functions of long coiled-coil proteins
    • Rose A, Meier I (2004) Scaffolds, levers, rods and springs: Diverse cellular functions of long coiled-coil proteins. Cell Mol Life Sci 61(16):1996-2009.
    • (2004) Cell Mol Life Sci , vol.61 , Issue.16 , pp. 1996-2009
    • Rose, A.1    Meier, I.2
  • 3
    • 0037335755 scopus 로고    scopus 로고
    • Molecular architecture of intermediate filaments
    • Strelkov SV, Herrmann H, Aebi U (2003) Molecular architecture of intermediate filaments. Bioessays 25(3):243-251.
    • (2003) Bioessays , vol.25 , Issue.3 , pp. 243-251
    • Strelkov, S.V.1    Herrmann, H.2    Aebi, U.3
  • 4
    • 34547516861 scopus 로고    scopus 로고
    • Hydrophobic association of {alpha}-helices, steric dewetting, and enthalpic barriers to protein folding
    • Maccallum JL et al. (2007) Hydrophobic association of {alpha}-helices, steric dewetting, and enthalpic barriers to protein folding. Proc Natl Acad Sci U S A 104(15):6206-6210.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.15 , pp. 6206-6210
    • Maccallum, J.L.1
  • 5
    • 0034653908 scopus 로고    scopus 로고
    • The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges
    • Burkhard P et al. (2000) The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges. Structure with Folding & Design 8(3):223-230.
    • (2000) Structure With Folding & Design , vol.8 , Issue.3 , pp. 223-230
    • Burkhard, P.1
  • 6
    • 0344628627 scopus 로고    scopus 로고
    • Historical review: Another 50th anniversary - New periodicities in coiled coils
    • Gruber M, Lupas AN (2003) Historical review: Another 50th anniversary - new periodicities in coiled coils. Trends Biochem Sci 28(12):679-685.
    • (2003) Trends Biochem Sci , vol.28 , Issue.12 , pp. 679-685
    • Gruber, M.1    Lupas, A.N.2
  • 7
    • 0021103673 scopus 로고
    • Periodic features in the amino-acid-sequence of nematode myosin rod
    • McLachlan AD, Karn J (1983) Periodic features in the amino-acid-sequence of nematode myosin rod. J Mol Biol 164(4):605-626.
    • (1983) J Mol Biol , vol.164 , Issue.4 , pp. 605-626
    • McLachlan, A.D.1    Karn, J.2
  • 8
    • 0029957901 scopus 로고    scopus 로고
    • Heptad breaks in alpha-helical coiled coils: Stutters and stammers
    • Brown JH, Cohen C, Parry DAD (1996) Heptad breaks in alpha-helical coiled coils: Stutters and stammers. Proteins 26(2):134-145.
    • (1996) Proteins , vol.26 , Issue.2 , pp. 134-145
    • Brown, J.H.1    Cohen, C.2    Parry, D.A.D.3
  • 9
    • 0037086445 scopus 로고    scopus 로고
    • Conserved segments 1A and 2B of the intermediate filament dimer: Their atomic structures and role in filament assembly
    • Strelkov SV et al. (2002) Conserved segments 1A and 2B of the intermediate filament dimer: Their atomic structures and role in filament assembly. EMBO J 21(6):1255-1266.
    • (2002) EMBO J , vol.21 , Issue.6 , pp. 1255-1266
    • Strelkov, S.V.1
  • 10
    • 0033618848 scopus 로고    scopus 로고
    • Intermediate filament assembly: Temperature sensitivity and polymorphism
    • Herrmann H, Aebi U (1999) Intermediate filament assembly: Temperature sensitivity and polymorphism. Cell Mol Life Sci 55(11):1416-1431.
    • (1999) Cell Mol Life Sci , vol.55 , Issue.11 , pp. 1416-1431
    • Herrmann, H.1    Aebi, U.2
  • 11
    • 0017849653 scopus 로고
    • Fibrinogen - Preliminary-analysis of amino-acid sequences of portions of alpha-chains, beta-chains and gamma-chains postulated to form interdomainal link between globular regions of molecule
    • Parry DAD (1978) Fibrinogen - preliminary-analysis of amino-acid sequences of portions of alpha-chains, beta-chains and gamma-chains postulated to form interdomainal link between globular regions of molecule. J Mol Biol 120(4):545-551.
    • (1978) J Mol Biol , vol.120 , Issue.4 , pp. 545-551
    • Parry, D.A.D.1
  • 13
    • 0036783392 scopus 로고    scopus 로고
    • Thermal folding and mechanical unfolding pathways of protein secondary structures
    • Cieplak M, Hoang TX, Robbins MO (2002) Thermal folding and mechanical unfolding pathways of protein secondary structures. Proteins 49(1):104-113.
    • (2002) Proteins , vol.49 , Issue.1 , pp. 104-113
    • Cieplak, M.1    Hoang, T.X.2    Robbins, M.O.3
  • 14
    • 0033064934 scopus 로고    scopus 로고
    • Unraveling proteins: A molecular mechanics study
    • Rohs R, Etchebest C, Lavery R (1999) Unraveling proteins: A molecular mechanics study. Biophys J 76(5):2760-2768.
    • (1999) Biophys J , vol.76 , Issue.5 , pp. 2760-2768
    • Rohs, R.1    Etchebest, C.2    Lavery, R.3
  • 15
    • 33645091911 scopus 로고    scopus 로고
    • Single molecule unzipping of coiled coils: Sequence resolved stability profiles
    • Bornschlogl T, Rief M (2006) Single molecule unzipping of coiled coils: sequence resolved stability profiles. Phys Rev Lett 96(11):118102.
    • (2006) Phys Rev Lett , vol.96 , Issue.11 , pp. 118102
    • Bornschlogl, T.1    Rief, M.2
  • 16
    • 0037569616 scopus 로고    scopus 로고
    • Mechanics of vimentin intermediate filaments
    • Wang N, Stamenovic D (2002) Mechanics of vimentin intermediate filaments. J Muscle Res Cell Motil 23(5-6):535-540.
    • (2002) J Muscle Res Cell Motil , vol.23 , Issue.5-6 , pp. 535-540
    • Wang, N.1    Stamenovic, D.2
  • 17
    • 0037297399 scopus 로고    scopus 로고
    • Modeling alpha-helical coiled-coil interactions: The axial and azimuthal alignment of 1B segments from vimentin intermediate filaments
    • Smith TA et al. (2003) Modeling alpha-helical coiled-coil interactions: the axial and azimuthal alignment of 1B segments from vimentin intermediate filaments. Proteins 50(2):207-212.
    • (2003) Proteins , vol.50 , Issue.2 , pp. 207-212
    • Smith, T.A.1
  • 18
    • 6344291659 scopus 로고    scopus 로고
    • Molecular mechanisms underlying the assembly of intermediate filaments
    • Kreplak L, Aebi U, Herrmann H (2004) Molecular mechanisms underlying the assembly of intermediate filaments. Exp Cell Res 301(1):77-83.
    • (2004) Exp Cell Res , vol.301 , Issue.1 , pp. 77-83
    • Kreplak, L.1    Aebi, U.2    Herrmann, H.3
  • 19
    • 0041319662 scopus 로고    scopus 로고
    • The mechanical properties of hydrated intermediate filaments: Insights from hagfish slime threads
    • Fudge DS et al. (2003) The mechanical properties of hydrated intermediate filaments: Insights from hagfish slime threads. Biophys J 85(3):2015-2027.
    • (2003) Biophys J , vol.85 , Issue.3 , pp. 2015-2027
    • Fudge, D.S.1
  • 20
    • 1042302712 scopus 로고    scopus 로고
    • Molecular design of the alpha-keratin composite: Insights from a matrix-free model, hagfish slime threads
    • Fudge DS, Gosline JM (2004) Molecular design of the alpha-keratin composite: Insights from a matrix-free model, hagfish slime threads. Proc R Soc Lond B Biol Sci 271(1536):291-299.
    • (2004) Proc R Soc Lond B Biol Sci , vol.271 , Issue.1536 , pp. 291-299
    • Fudge, D.S.1    Gosline, J.M.2
  • 21
    • 0035201307 scopus 로고    scopus 로고
    • The structure and function of nuclear lamins: Implications for disease
    • Moir RD, Spann TP (2001) The structure and function of nuclear lamins: implications for disease. Cell Mol Life Sci 58(12-13):1748-1757.
    • (2001) Cell Mol Life Sci , vol.58 , Issue.12-13 , pp. 1748-1757
    • Moir, R.D.1    Spann, T.P.2
  • 22
    • 0035831041 scopus 로고    scopus 로고
    • Lamins and disease: Insights into nuclear infrastructure
    • Wilson KL, Zastrow MS, Lee KK (2001) Lamins and disease: Insights into nuclear infrastructure. Cell 104(5): 647-650.
    • (2001) Cell , vol.104 , Issue.5 , pp. 647-650
    • Wilson, K.L.1    Zastrow, M.S.2    Lee, K.K.3
  • 23
    • 0034308278 scopus 로고    scopus 로고
    • The 'ins' and 'outs' of intermediate filament organization
    • Coulombe PA et al. (2000) The 'ins' and 'outs' of intermediate filament organization. Trends Cell Biol 10(10):420-428.
    • (2000) Trends Cell Biol , vol.10 , Issue.10 , pp. 420-428
    • Coulombe, P.A.1
  • 24
    • 27744588225 scopus 로고    scopus 로고
    • Exploring the mechanical behavior of single intermediate filaments
    • Kreplak L et al. (2005) Exploring the mechanical behavior of single intermediate filaments. J Mol Biol 354(3):569-577.
    • (2005) J Mol Biol , vol.354 , Issue.3 , pp. 569-577
    • Kreplak, L.1
  • 25
    • 33747798639 scopus 로고    scopus 로고
    • Nanomechanical properties of desmin intermediate filaments
    • Kiss B, Karsai A, Kellermayer MSZ (2006) Nanomechanical properties of desmin intermediate filaments. J Struct Biol 155(2):327-339.
    • (2006) J Struct Biol , vol.155 , Issue.2 , pp. 327-339
    • Kiss, B.1    Karsai, A.2    Kellermayer, M.S.Z.3
  • 26
    • 6344273968 scopus 로고    scopus 로고
    • Mechanisms of disease: Intermediate filament proteins and their associated diseases
    • Omary MB, Coulombe PA, McLean WHI (2004) Mechanisms of disease: intermediate filament proteins and their associated diseases. N Engl J Med 351(20):2087-2100.
    • (2004) N Engl J Med , vol.351 , Issue.20 , pp. 2087-2100
    • Omary, M.B.1    Coulombe, P.A.2    McLean, W.H.I.3
  • 27
    • 30344444789 scopus 로고    scopus 로고
    • Mutations in vimentin disrupt the cytoskeleton in fibroblasts and delay execution of apoptosis
    • Schietke R et al. (2006) Mutations in vimentin disrupt the cytoskeleton in fibroblasts and delay execution of apoptosis. Eur J Cell Biol 85(1):1-10.
    • (2006) Eur J Cell Biol , vol.85 , Issue.1 , pp. 1-10
    • Schietke, R.1
  • 28
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • Herrmann H, Aebi U (2004) Intermediate filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds. Ann Rev Biochem 73:749-789.
    • (2004) Ann Rev Biochem , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 29
    • 34548407835 scopus 로고    scopus 로고
    • Superelasticity, energy dissipation and strain hardening of vimentin coiled-coil intermediate filaments: Atomistic and continuum studies
    • Ackbarow T, Buehler MJ (2007) Superelasticity, energy dissipation and strain hardening of vimentin coiled-coil intermediate filaments: atomistic and continuum studies. J Mater Sci 42:8771-8787.
    • (2007) J Mater Sci , vol.42 , pp. 8771-8787
    • Ackbarow, T.1    Buehler, M.J.2
  • 30
    • 0018101150 scopus 로고
    • Models for specific adhesion of cells to cells
    • Bell GI (1978) Models for specific adhesion of cells to cells. Science 200(4342):618-627.
    • (1978) Science , vol.200 , Issue.4342 , pp. 618-627
    • Bell, G.I.1
  • 31
    • 8344276781 scopus 로고    scopus 로고
    • NAMD: A parallel, object oriented molecular dynamics program
    • Nelson MT et al. (1996) NAMD: A parallel, object oriented molecular dynamics program. Int J Supercomput Appl High Perform Comput 10(4):251-268.
    • (1996) Int J Supercomput Appl High Perform Comput , vol.10 , Issue.4 , pp. 251-268
    • Nelson, M.T.1
  • 32
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell AD et al. (1998) All-atom empirical potential for molecular modeling and dynamics studies of proteins. J Phys Chem B 102(18):3586-3616.
    • (1998) J Phys Chem B , vol.102 , Issue.18 , pp. 3586-3616
    • MacKerell, A.D.1
  • 33
    • 0031848099 scopus 로고    scopus 로고
    • Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation
    • Lu H et al. (1998) Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation. Biophys J 75(2):662-671.
    • (1998) Biophys J , vol.75 , Issue.2 , pp. 662-671
    • Lu, H.1
  • 35
    • 0036977558 scopus 로고    scopus 로고
    • The myosin coiled-coil is a truly elastic protein structure
    • Schwaiger I et al. (2002) The myosin coiled-coil is a truly elastic protein structure. Nat Mater 1(4):232-235.
    • (2002) Nat Mater , vol.1 , Issue.4 , pp. 232-235
    • Schwaiger, I.1
  • 37
    • 33845202460 scopus 로고    scopus 로고
    • On the mechanics of mother-of-pearl: A key feature in the material hierarchical structure
    • Barthelat F et al. (2007) On the mechanics of mother-of-pearl: A key feature in the material hierarchical structure. J Mech Phys Solids 55(2):306-337.
    • (2007) J Mech Phys Solids , vol.55 , Issue.2 , pp. 306-337
    • Barthelat, F.1
  • 38
    • 0031899035 scopus 로고    scopus 로고
    • Artificial fibrous proteins: A review
    • Heslot H (1998) Artificial fibrous proteins: A review. Biochimie 80(1):19-31.
    • (1998) Biochimie , vol.80 , Issue.1 , pp. 19-31
    • Heslot, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.