| Year |
Citation |
Score |
| 2013 |
Damnjanovic B, Weber A, Potschies M, Greie JC, Apell HJ. Mechanistic analysis of the pump cycle of the KdpFABC P-type ATPase. Biochemistry. 52: 5563-76. PMID 23930894 DOI: 10.1021/Bi400729E |
0.346 |
|
| 2003 |
WEBER A. The ultracentrifugal separation of L-myosin and actin in an actomyosin sol under the influence of ATP. Biochimica Et Biophysica Acta. 19: 345-51. PMID 13315282 DOI: 10.1016/0006-3002(56)90439-5 |
0.328 |
|
| 1999 |
Weber A, Pennise CR, Fowler VM. Tropomodulin increases the critical concentration of barbed end-capped actin filaments by converting ADP · P(i)-actin to ADP-actin at all pointed filament ends Journal of Biological Chemistry. 274: 34637-34645. PMID 10574928 DOI: 10.1074/Jbc.274.49.34637 |
0.489 |
|
| 1999 |
Weber A. Actin binding proteins that change extent and rate of actin monomer-polymer distribution by different mechanisms. Molecular and Cellular Biochemistry. 190: 67-74. DOI: 10.1007/978-1-4615-5543-8_8 |
0.598 |
|
| 1995 |
Freeman NL, Chen Z, Horenstein J, Weber A, Field J. An Actin Monomer Binding Activity Localizes to the Carboxyl-terminal Half of the Saccharomyces cerevisiae Cyclase-associated Protein Journal of Biological Chemistry. 270: 5680-5685. PMID 7890691 DOI: 10.1074/Jbc.270.10.5680 |
0.534 |
|
| 1995 |
Gregorio CC, Weber A, Bondad M, Pennise CR, Fowler VM. Requirement of pointed-end capping by tropomodulin to maintain actin filament length in embryonic chick cardiac myocytes. Nature. 377: 83-6. PMID 7544875 DOI: 10.1038/377083A0 |
0.546 |
|
| 1994 |
Weber A, Pennise CR, Pring M. DNase I increases the rate constant of depolymerization at the pointed (-) end of actin filaments. Biochemistry. 33: 4780-4786. PMID 8161537 DOI: 10.1021/Bi00182A005 |
0.609 |
|
| 1994 |
Weber A, Pennise CR, Babcock GG, Fowler VM. Tropomodulin caps the pointed ends of actin filaments Journal of Cell Biology. 127: 1627-1635. PMID 7798317 DOI: 10.1083/Jcb.127.6.1627 |
0.555 |
|
| 1992 |
Pring M, Weber A, Bubb MR. Profilin-actin complexes directly elongate actin filaments at the barbed end. Biochemistry. 31: 1827-36. PMID 1737036 DOI: 10.1021/bi00121a035 |
0.448 |
|
| 1992 |
Weber A, Nachmias VT, Pennise CR, Pring M, Safer D. Interaction of thymosin beta 4 with muscle and platelet actin: implications for actin sequestration in resting platelets. Biochemistry. 31: 6179-6185. PMID 1627561 DOI: 10.1021/Bi00142A002 |
0.451 |
|
| 1992 |
Tilney LG, DeRosier DJ, Weber A, Tilney MS. How Listeria exploits host cell actin to form its own cytoskeleton. II. Nucleation, actin filament polarity, filament assembly, and evidence for a pointed end capper. The Journal of Cell Biology. 118: 83-93. PMID 1618909 DOI: 10.1083/Jcb.118.1.83 |
0.517 |
|
| 1991 |
Weber A, Pring M, Lin SL, Bryan J. Role of the N- and C-terminal actin-binding domains of gelsolin in barbed filament end capping Biochemistry. 30: 9327-9334. PMID 1654094 DOI: 10.1021/Bi00102A027 |
0.583 |
|
| 1990 |
Young CL, Southwick FS, Weber A. Kinetics of the interaction of a 41-kilodalton macrophage capping protein with actin: promotion of nucleation during prolongation of the lag period. Biochemistry. 29: 2232-40. PMID 2337601 DOI: 10.1021/Bi00461A005 |
0.588 |
|
| 1989 |
Broschat KO, Weber A, Burgess DR. Tropomyosin stabilizes the pointed end of actin filaments by slowing depolymerization. Biochemistry. 28: 8501-8506. PMID 2605200 DOI: 10.1021/Bi00447A035 |
0.495 |
|
| 1987 |
Weber A, Northrop J, Bishop MF, Ferrone FA, Mooseker MS. Kinetics of actin elongation and depolymerization at the pointed end. Biochemistry. 26: 2537-44. PMID 3607031 DOI: 10.1021/Bi00383A020 |
0.528 |
|
| 1987 |
Weber A, Northrop J, Bishop MF, Ferrone FA, Mooseker MS. Nucleation of actin polymerization by villin and elongation at subcritical monomer concentration. Biochemistry. 26: 2528-36. PMID 3607030 DOI: 10.1021/Bi00383A019 |
0.556 |
|
| 1986 |
Carson M, Weber A, Zigmond SH. An actin-nucleating activity in polymorphonuclear leukocytes is modulated by chemotactic peptides. The Journal of Cell Biology. 103: 2707-14. PMID 3793753 DOI: 10.1083/Jcb.103.6.2707 |
0.346 |
|
| 1986 |
Knox MK, Szent-Györgyi AG, Trueblood CE, Weber A, Zigmond S. The effect of low ATP concentrations on relaxation in the myosin regulated myofibrils from scallop. Journal of Muscle Research and Cell Motility. 7: 110-4. PMID 2940259 DOI: 10.1007/Bf01753411 |
0.451 |
|
| 1985 |
Walsh TP, Weber A, Davis K, Bonder E, Mooseker M. Calcium dependence of villin-induced actin depolymerization. Biochemistry. 23: 6099-102. PMID 6525347 DOI: 10.1021/Bi00320A030 |
0.497 |
|
| 1985 |
Walsh TP, Trueblood CE, Evans R, Weber A. Removal of tropomyosin overlap and the co-operative response to increasing calcium concentrations of the acto-subfragment-1 ATPase☆ Journal of Molecular Biology. 182: 265-269. PMID 3158745 DOI: 10.1016/0022-2836(85)90344-4 |
0.316 |
|
| 1984 |
Walsh TP, Weber A, Higgins J, Bonder EM, Mooseker MS. Effect of villin on the kinetics of actin polymerization Biochemistry. 23: 2613-2621. PMID 6432033 DOI: 10.1021/Bi00307A012 |
0.59 |
|
| 1982 |
Murray JM, Knox MK, Trueblood CE, Weber A. Potentiated state of the tropomyosin actin filament and nucleotide-containing myosin subfragment 1. Biochemistry. 21: 906-915. PMID 6462176 DOI: 10.1021/Bi00534A015 |
0.624 |
|
| 1981 |
Murray JM, Weber A. Cooperativity of the calcium switch of regulated rabbit actomyosin system Molecular and Cellular Biochemistry. 35: 11-15. PMID 6452574 DOI: 10.1007/Bf02358183 |
0.414 |
|
| 1981 |
Murray JM, Weber A, Knox MK. Myosin subfragment 1 binding to relaxed actin filaments and steric model of relaxation. Biochemistry. 20: 641-649. PMID 6452158 DOI: 10.1021/Bi00506A030 |
0.67 |
|
| 1981 |
Murray J, Weber A, Knox M. Corrections - Myosin Subfragment 1 Binding to Relaxed Actin Filaments and Steric Model of Relaxation Biochemistry. 20: 5094-5094. DOI: 10.1021/Bi00520A605 |
0.668 |
|
| 1980 |
Murray JM, Knox MK, Trueblood CE, Weber A. Do tropomyosin and myosin compete for actin sites in the presence of calcium Febs Letters. 114: 169-173. PMID 6892903 DOI: 10.1016/0014-5793(80)80886-6 |
0.486 |
|
| 1979 |
Porter M, Weber A. Non-cooperative response of actin-cystein 373 in cooperatively behaving regulated actin filaments. Febs Letters. 105: 259-262. PMID 158543 DOI: 10.1016/0014-5793(79)80624-9 |
0.515 |
|
| 1976 |
Pemrick S, Weber A. Mechanism of inhibition of relaxation by N-ethylmaleimide treatment of myosin. Biochemistry. 15: 5193-5198. PMID 136272 DOI: 10.1021/Bi00668A038 |
0.438 |
|
| 1975 |
Bremel RD, Weber A. Calcium binding to rabbit skeletal myosin under physiological conditions. Biochimica Et Biophysica Acta. 376: 366-374. PMID 1115783 DOI: 10.1016/0005-2728(75)90028-6 |
0.435 |
|
| 1975 |
Loscalzo J, Reed GH, Weber A. Conformational change and cooperativity in actin filaments free of tropomyosin Proceedings of the National Academy of Sciences of the United States of America. 72: 3412-3415. PMID 1103145 DOI: 10.1073/Pnas.72.9.3412 |
0.42 |
|
| 1975 |
Marston S, Weber A. The dissociation constant of the actin-heavy meromyosin subfragment-1 complex. Biochemistry. 14: 3868-73. PMID 126077 DOI: 10.1021/Bi00688A021 |
0.646 |
|
| 1973 |
Bremel RD, Murray JM, Weber A. Manifestations of Cooperative Behavior in the Regulated Actin Filament during Actin-Activated ATP Hydrolysis in the Presence of Calcium Cold Spring Harbor Symposia On Quantitative Biology. 37: 267-275. DOI: 10.1101/Sqb.1973.037.01.037 |
0.617 |
|
| 1972 |
Bremel RD, Weber A. Cooperation within actin filament in vertebrate skeletal muscle. Nature: New Biology. 238: 97-101. PMID 4261616 DOI: 10.1038/NEWBIO238097A0 |
0.327 |
|
| 1972 |
Maruyama K, Weber A. Binding of adenosine triphosphate to myofibrils during contraction and relaxation. Biochemistry. 11: 2990-2998. PMID 4261261 DOI: 10.1021/Bi00766A010 |
0.443 |
|
| 1969 |
Weber A, Herz R, Reiss I. The role of magnesium in the relaxation of myofibrils. Biochemistry. 8: 2266-2271. PMID 4240513 DOI: 10.1021/Bi00834A005 |
0.307 |
|
| 1969 |
Weber A. Parallel response of myofibrillar contraction and relaxation to four different nucleoside triphophates. The Journal of General Physiology. 53: 781-91. PMID 4239137 DOI: 10.1085/JGP.53.6.781 |
0.312 |
|
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