다음과 같은 기능을 한번의 로그인으로 사용 할 수 있습니다.
NTIS 바로가기
RSC advances, v.6 no.116, 2016년, pp.115252 - 115270
Modarres, H. Pezeshgi (Molecular Cell Biomechanics Laboratory) , Mofrad, M. R. (Molecular Cell Biomechanics Laboratory) , Sanati-Nezhad, A. (BioMEMS and Bioinspired Microfluidic Laboratory)
AI-Helper
The use of enzymes for industrial and biomedical applications is limited to their function at elevated temperatures. The principles of thermostability engineering need to be implemented for proteins with low thermal stability to broaden their applications. Therefore, understanding the thermal stabil...
Biophys. J. Ghosh 99 3996 2010 10.1016/j.bpj.2010.10.036
J. Biol. Chem. Park 291 1692 2016 10.1074/jbc.M115.674408
Stability of protein pharmaceuticals, part A. Chemical and physical pathways of protein degradation Volkin 1992 D. Volkin and C.Middaugh, Stability of protein pharmaceuticals, part A. Chemical and physical pathways of protein degradation, Plenum Press, New York, NY, 1992, pp. 215-247
Hum. Mutat. Khan 31 675 2010 10.1002/humu.21242
Curr. Opin. Biotechnol. Lewin 24 516 2013 10.1016/j.copbio.2012.10.012
Extremophiles Tazi 18 525 2014 10.1007/s00792-014-0637-x
Microbiol. Mol. Biol. Rev. Vieille 65 1 2001 10.1128/MMBR.65.1.1-43.2001
Appl. Environ. Microbiol. Brown 59 2614 1993 10.1128/AEM.59.8.2614-2621.1993
Biochemistry Jaenicke 63 312 1998
J. Mol. Biol. Vogt 269 631 1997 10.1006/jmbi.1997.1042
FEBS Lett. Chakravarty 470 65 2000 10.1016/S0014-5793(00)01267-9
Appl. Biochem. Biotechnol. Pack 171 1212 2013 10.1007/s12010-013-0195-1
Appl. Environ. Microbiol. Vieille 61 1867 1995 10.1128/AEM.61.5.1867-1875.1995
Proteins: Struct., Funct., Bioinf. Maes 37 441 1999 10.1002/(SICI)1097-0134(19991115)37:3<441::AID-PROT11>3.0.CO;2-7
Biochemistry Bauer 37 17170 1998 10.1021/bi9814944
Biochemistry Argos 18 5698 1979 10.1021/bi00592a028
Int. J. Pept. Protein Res. Gerald 43 97 1994 10.1111/j.1399-3011.1994.tb00380.x
Amino Acids Zhou 34 25 2008 10.1007/s00726-007-0589-x
FEBS Lett. Chakravarty 470 65 2000 10.1016/S0014-5793(00)01267-9
Protein Eng. Kumar 13 179 2000 10.1093/protein/13.3.179
Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol. Panasik 1543 189 2000 10.1016/S0167-4838(00)00182-5
J. Biotechnol. Pack 111 269 2004 10.1016/j.jbiotec.2004.01.018
Biophys. Chem. Sadeghi 119 256 2006 10.1016/j.bpc.2005.09.018
Proc. Natl. Acad. Sci. U. S. A. Van den Burg 95 2056 1998 10.1073/pnas.95.5.2056
J. Bacteriol. Xu 185 4038 2003 10.1128/JB.185.14.4038-4049.2003
Protein Sci. Catanzano 6 1682 1997 10.1002/pro.5560060808
Biophys. Chem. Gromiha 82 51 1999 10.1016/S0301-4622(99)00103-9
Genet. Mol. Res. Trivedi 5 816 2006
Structure Szilágyi 8 493 2000 10.1016/S0969-2126(00)00133-7
J. Mol. Biol. Fukuchi 327 347 2003 10.1016/S0022-2836(03)00150-5
J. Biochem. Nakashima 133 507 2003 10.1093/jb/mvg067
Genome Res. Saunders 13 1580 2003 10.1101/gr.1180903
J. Biol. Chem. Suhre 278 17198 2003 10.1074/jbc.M301327200
J. Biol. Chem. Tanaka 279 32957 2004 10.1074/jbc.M404405200
Genet. Mol. Res. Farias 2 383 2003
Proc. Natl. Acad. Sci. U. S. A. Kawashima 97 14257 2000 10.1073/pnas.97.26.14257
Proc. Natl. Acad. Sci. U. S. A. Fütterer 101 9091 2004 10.1073/pnas.0401356101
PLoS Comput. Biol. Zeldovich 3 62 2007 10.1371/journal.pcbi.0030062
Proteins: Struct., Funct., Bioinf. Liang 59 58 2005 10.1002/prot.20386
Biophys. Chem. Gromiha 82 51 1999 10.1016/S0301-4622(99)00103-9
FEBS Lett. Dombkowski 588 206 2014 10.1016/j.febslet.2013.11.024
Protein Eng. Chirakkal 14 161 2001 10.1093/protein/14.3.161
Journal of Neuroimmune Pharmacology Gilmore 3 83 2008 10.1007/s11481-007-9099-6
Protein Sci. Bueno 15 1858 2006 10.1110/ps.062274906
Proteins Gromiha 81 715 2013 10.1002/prot.24232
Nat. Struct. Biol. Northey 9 126 2002 10.1038/nsb748
Eur. Biophys. J. Biophys. Lett. Banerji 38 577 2009 10.1007/s00249-009-0409-1
Protein Eng. Kono 11 47 1998 10.1093/protein/11.1.47
Biochemistry Chen 40 14004 2001 10.1021/bi011268l
Sci. Rep. Pucci 6 23257 2016 10.1038/srep23257
Biochemistry Kellis 28 4914 1989 10.1021/bi00437a058
J. Mol. Biol. Baldwin 259 542 1996 10.1006/jmbi.1996.0338
J. Mol. Biol. Anil 354 693 2005 10.1016/j.jmb.2005.08.054
Biochemistry Buckle 35 4298 1996 10.1021/bi9524676
Biochemistry Otzen 34 13051 1995 10.1021/bi00040a016
J. Biomol. Struct. Dyn. Priyakumar 29 961 2012 10.1080/07391102.2012.10507415
Biochemistry Li 37 10563 1998 10.1021/bi973006i
Int. J. Biol. Macromol. Pack 35 169 2005 10.1016/j.ijbiomac.2005.01.007
Bioinformatics Glyakina 23 2231 2007 10.1093/bioinformatics/btm345
Appl. Environ. Microbiol. Dong 63 3569 1997 10.1128/AEM.63.9.3569-3576.1997
J. Mol. Biol. Ishikawa 230 529 1993 10.1006/jmbi.1993.1169
Pept. Sci. Waters 76 435 2004 10.1002/bip.20144
Protein Eng. Bhattacharyya 15 91 2002 10.1093/protein/15.2.91
Proteins: Struct., Funct., Bioinf. Thomas 48 635 2002 10.1002/prot.10191
Curr. Opin. Chem. Biol. Waters 6 736 2002 10.1016/S1367-5931(02)00359-9
J. Am. Chem. Soc. Butterfield 124 9751 2002 10.1021/ja026668q
Biochemistry Padmanabhan 37 17318 1998 10.1021/bi9813678
Biochemistry Viguera 34 8771 1995 10.1021/bi00027a028
Protein Sci. Stapley 4 2383 1995 10.1002/pro.5560041117
Angew. Chem. Espinosa 112 2420 2000 10.1002/1521-3757(20000703)112:13<2420::AID-ANGE2420>3.0.CO;2-8
J. Mol. Biol. Honda 295 269 2000 10.1006/jmbi.1999.3346
Acc. Chem. Res. Smith 30 153 1997 10.1021/ar9601048
FASEB J. Gazit 16 77 2002 10.1096/fj.01-0442hyp
Proc. Natl. Acad. Sci. U. S. A. Cochran 98 5578 2001 10.1073/pnas.091100898
J. Am. Chem. Soc. Skalicky 121 4941 1999 10.1021/ja983309f
FEBS J. Souza 238 1124 2016 10.1111/febs.13659
Protein Sci. Tatko 12 2443 2003 10.1110/ps.03284003
J. Am. Chem. Soc. Andrew 124 12706 2002 10.1021/ja027629h
J. Am. Chem. Soc. Shi 124 3284 2002 10.1021/ja0174938
J. Mol. Biol. de Bakker 285 1811 1999 10.1006/jmbi.1998.2397
Biochemistry Dill 29 7133 1990 10.1021/bi00483a001
J. Am. Chem. Soc. Thomas 126 2208 2004 10.1021/ja039159c
Biochemistry Anderson 29 2403 1990 10.1021/bi00461a025
Extremophiles Saelensminde 13 11 2009 10.1007/s00792-008-0192-4
PLoS Comput. Biol. Berezovsky 3 e52 2007 10.1371/journal.pcbi.0030052
Proc. Natl. Acad. Sci. U. S. A. Halskau Jr 105 8625 2008 10.1073/pnas.0709881105
Proc. Natl. Acad. Sci. U. S. A. Matthews 84 6663 1987 10.1073/pnas.84.19.6663
Protein Eng. Sriprapundh 13 259 2000 10.1093/protein/13.4.259
Biochemistry Nakai 38 2413 1999 10.1021/bi9819881
Eur. J. Biochem. Watanabe 226 277 1994 10.1111/j.1432-1033.1994.tb20051.x
Biochem. Biophys. Res. Commun. Rahman 248 920 1998 10.1006/bbrc.1998.8933
Proc. Natl. Acad. Sci. U. S. A. Vetriani 95 12300 1998 10.1073/pnas.95.21.12300
Protein Sci. Neet 3 2167 1994 10.1002/pro.5560031202
Nature Nicholson 336 651 1988 10.1038/336651a0
Biosci., Biotechnol., Biochem. Harada 71 2952 2007 10.1271/bbb.70354
Structure Grabarse 7 1257 1999 10.1016/S0969-2126(00)80059-3
Eur. J. Biochem. Kojoh 264 85 1999 10.1046/j.1432-1327.1999.00579.x
Arch. Microbiol. Shima 170 469 1998 10.1007/s002030050669
Eur. J. Biochem. Shima 258 85 1998 10.1046/j.1432-1327.1998.2580085.x
Eur. J. Biochem. Wilquet 255 628 1998 10.1046/j.1432-1327.1998.2550628.x
Protein Eng. Facchiano 11 753 1998 10.1093/protein/11.9.753
Biochemistry Kawamura 35 1195 1996 10.1021/bi951581l
J. Mol. Biol. Nojima 116 429 1977 10.1016/0022-2836(77)90078-X
Biochemistry Pezeshgi Modarres 3076 2015 10.1021/bi501227b
Enzyme Microb. Technol. Ó’Fágáin 33 137 2003 10.1016/S0141-0229(03)00160-1
Proc. Natl. Acad. Sci. U. S. A. Chen 90 5618 1993 10.1073/pnas.90.12.5618
Proc. Natl. Acad. Sci. U. S. A. Stemmer 91 10747 1994 10.1073/pnas.91.22.10747
Biotechnol. Bioeng. Morawski 76 99 2001 10.1002/bit.1149
Biomol. Eng. Eijsink 22 21 2005 10.1016/j.bioeng.2004.12.003
Methods Mol. Biol. Matsuura 182 221 2002
Enzyme Microb. Technol. Liu 28 582 2001 10.1016/S0141-0229(00)00349-5
Biotechnol. Lett. Gomez 22 1191 2000 10.1023/A:1005645531521
Enzyme Microb. Technol. Khajeh 28 543 2001 10.1016/S0141-0229(01)00296-4
FEBS J. Socha 280 5582 2013 10.1111/febs.12354
Protein Chromatography Ó’Fágáin 101 2017 10.1007/978-1-4939-6412-3_7
Hum. Mutat. Thusberg 30 703 2009 10.1002/humu.20938
Curr. Opin. Struct. Biol. Wijma 23 588 2013 10.1016/j.sbi.2013.04.008
Biotechnol. J. Chaparro-Riggers 2 180 2007 10.1002/biot.200600170
Biotechnol. J. Polizzi 1 531 2006 10.1002/biot.200600029
ChemBioChem Vazquez-Figueroa 8 2295 2007 10.1002/cbic.200700500
Biochim. Biophys. Acta Lehmann 1543 408 2000 10.1016/S0167-4838(00)00238-7
Protein Eng. Lehmann 15 403 2002 10.1093/protein/15.5.403
Appl. Environ. Microbiol. Anbar 78 3458 2012 10.1128/AEM.07985-11
J. Biotechnol. Blum 160 214 2012 10.1016/j.jbiotec.2012.02.014
Protein Eng., Des. Sel. Vazquez-Figueroa 21 673 2008 10.1093/protein/gzn048
Curr. Opin. Biotechnol. Lehmann 12 371 2001 10.1016/S0958-1669(00)00229-9
Protein Eng., Des. Sel. Porebski 1 2016
Protein Eng. Lehmann 13 49 2000 10.1093/protein/13.1.49
Proc. Natl. Acad. Sci. U. S. A. Kohl 100 1700 2003 10.1073/pnas.0337680100
Proc. Natl. Acad. Sci. U. S. A. Mosavi 99 16029 2002 10.1073/pnas.252537899
ChemBioChem Forrer 5 183 2004 10.1002/cbic.200300762
Structure Tripp 11 486 2003 10.1016/S0969-2126(03)00078-9
Protein Design Kajander 151 2006 10.1385/1-59745-116-9:151
Protein Eng., Des. Sel. Amin 17 787 2004 10.1093/protein/gzh091
Protein Eng., Des. Sel. Jacobs 25 107 2012 10.1093/protein/gzr064
Protein Eng., Des. Sel. Dai 20 69 2007 10.1093/protein/gzl056
Biotechnol. J. Polizzi 1 531 2006 10.1002/biot.200600029
ChemBioChem Vázquez-Figueroa 8 2295 2007 10.1002/cbic.200700500
J. Biotechnol. Blum 160 214 2012 10.1016/j.jbiotec.2012.02.014
Biochemistry Pantoliano 28 7205 1989 10.1021/bi00444a012
J. Mol. Biol. Steipe 240 188 1994 10.1006/jmbi.1994.1434
Protein Eng. Steipe 388 176 2004 10.1016/S0076-6879(04)88016-9
Biochemistry Pantoliano 28 7205 1989 10.1021/bi00444a012
Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol. Lehmann 1543 408 2000 10.1016/S0167-4838(00)00238-7
Protein Eng. Lehmann 15 403 2002 10.1093/protein/15.5.403
Methods Enzymol. Durani 523 237 2013 10.1016/B978-0-12-394292-0.00011-4
Biochemistry Dietrich 51 5633 2012 10.1021/bi300747r
J. Mol. Biol. Sullivan 420 384 2012 10.1016/j.jmb.2012.04.025
J. Mol. Biol. Sullivan 413 195 2011 10.1016/j.jmb.2011.08.001
Appl. Environ. Microbiol. Xiao 74 1183 2008 10.1128/AEM.02220-07
Appl. Environ. Microbiol. Wang 80 2158 2014 10.1128/AEM.03458-13
J. Biotechnol. Li 210 8 2015 10.1016/j.jbiotec.2015.06.406
Org. Biomol. Chem. Huang 9 4138 2011 10.1039/c0ob00972e
J. Biotechnol. Joo 151 56 2011 10.1016/j.jbiotec.2010.10.002
Biochemistry Meharenna 49 6680 2010 10.1021/bi100929x
J. Mol. Graphics Modell. Kundu 28 820 2010 10.1016/j.jmgm.2010.03.001
J. Mol. Graphics Modell. Kundu 27 871 2009 10.1016/j.jmgm.2009.01.004
Protein Pept. Lett. Rahman 16 1360 2009 10.2174/092986609789353763
J. Mol. Model. Spiwok 13 485 2007 10.1007/s00894-006-0164-5
Protein Eng., Des. Sel. Purmonen 20 551 2007 10.1093/protein/gzm056
J. Biotechnol. Chen 164 354 2013 10.1016/j.jbiotec.2013.01.021
J. Ind. Microbiol. Biotechnol. Fei 40 457 2013 10.1007/s10295-013-1260-z
Protein Eng. Pikkemaat 15 185 2002 10.1093/protein/15.3.185
Biotechnol. Bioeng. Badieyan 109 31 2012 10.1002/bit.23280
Biotechnol. Bioeng. Le 109 867 2012 10.1002/bit.24371
FEBS J. Tian 277 4901 2010 10.1111/j.1742-4658.2010.07895.x
J. Biotechnol. Joo 146 31 2010 10.1016/j.jbiotec.2009.12.021
Enzyme Microb. Technol. Kim 47 1 2010 10.1016/j.enzmictec.2010.04.003
Biotechnol. Prog. Kim 26 1038 2010 10.1002/btpr.408
Enzyme Microb. Technol. Kim 47 1 2010 10.1016/j.enzmictec.2010.04.003
Enzyme Microb. Technol. Zhang 50 325 2012 10.1016/j.enzmictec.2012.03.002
Biophys. Chem. Siglioccolo 153 104 2010 10.1016/j.bpc.2010.10.009
Biotechnol. Adv. Yu 32 308 2014 10.1016/j.biotechadv.2013.10.012
Protein Eng., Des. Sel. Touw 27 457 2014 10.1093/protein/gzu044
Nat. Protoc. Reetz 2 891 2007 10.1038/nprot.2007.72
Cell. Mol. Life Sci. Teilum 66 2231 2009 10.1007/s00018-009-0014-6
Supercomputing for Molecular Dynamics Simulations Heinecke 2015 10.1007/978-3-319-17148-7 A. Heinecke , W.Eckhardt, M.Horsch and H.-J.Bungartz, in Supercomputing for Molecular Dynamics Simulations, Springer, 2015, pp. 11-29
Molecular Modeling of Proteins Lopes 47 2015 10.1007/978-1-4939-1465-4_3
Appl. Biochem. Biotechnol. Zhu 178 725 2016 10.1007/s12010-015-1905-7
Protein Eng., Des. Sel. Purmonen 20 551 2007 10.1093/protein/gzm056
Protein Pept. Lett. Abdul Rahman 16 1360 2009 10.2174/092986609789353763
Protein J. Karjiban 28 14 2009 10.1007/s10930-008-9159-7
Protein Pept. Lett. Abedi Karjiban 17 699 2010 10.2174/092986610791190345
Proteins: Struct., Funct., Bioinf. D'Auria 38 351 2000 10.1002/(SICI)1097-0134(20000301)38:4<351::AID-PROT1>3.0.CO;2-6
J. Mol. Biol. Wintrode 327 745 2003 10.1016/S0022-2836(03)00147-5
Biophys. J. Fitter 79 1629 2000 10.1016/S0006-3495(00)76413-7
Bioinformation Sharma 3 10 430 2009 10.6026/97320630003430
Mol. Phys. Vieira 107 59 2009 10.1080/00268970902717959
J. Biol. Chem. Bae 280 30943 2005 10.1074/jbc.M504216200
Biochim. Biophys. Acta, Proteins Proteomics Vemparala 1814 630 2011 10.1016/j.bbapap.2011.03.012
J. Mol. Graphics Modell. Kundu 28 820 2010 10.1016/j.jmgm.2010.03.001
J. Mol. Model. Yu 18 2869 2012 10.1007/s00894-011-1308-9
Chin. J. Chem. Phys. Xu 22 467 2009 10.1088/1674-0068/22/05/467-472
J. Mol. Model. Mazola 21 1 2015 10.1007/s00894-015-2772-4
J. Mol. Model. Kumar 21 1 2015 10.1007/s00894-015-2696-z
J. Phys. Chem. B Singh 119 392 2015 10.1021/jp5079554
Appl. Environ. Microbiol. Tu 81 6938 2015 10.1128/AEM.01363-15
Biochemistry Yin 79 531 2014
Protein J. Noorbatcha 32 309 2013 10.1007/s10930-013-9489-y
PLoS One Christensen 8 e61985 2013 10.1371/journal.pone.0061985
J. Biomol. Struct. Dyn. Chen 1 2016
J. Comput. Chem. Phillips 26 1781 2005 10.1002/jcc.20289
Molecular Modeling Annual Lindahl 7 306 2001 10.1007/s008940100045
J. Comput. Chem. Brooks 30 1545 2009 10.1002/jcc.21287
J. Comput. Chem. Case 26 1668 2005 10.1002/jcc.20290
J. Non-Cryst. Solids Kalimeri 407 494 2015 10.1016/j.jnoncrysol.2014.07.005
J. Chem. Inf. Model. Pfleger 53 1007 2013 10.1021/ci400044m
Bioinformatics Rathi 31 2394 2015 10.1093/bioinformatics/btv139
Nucleic Acids Res. Krüger gkt292 2013
PLoS One Rathi 10 e0130289 2015 10.1371/journal.pone.0130289
Rigidity Theory and Applications Jacobs 2002 D. J. Jacobs , L. A.Kuhn and M. F.Thorpe, in Rigidity Theory and Applications, Springer, 2002, pp. 357-384
Proteins: Struct., Funct., Bioinf. Ahmed 63 1038 2006 10.1002/prot.20907
Phys. Biol. Rader 7 016002 2009 10.1088/1478-3975/7/1/016002
J. Biotechnol. Rathi 159 135 2012 10.1016/j.jbiotec.2012.01.027
Curr. Protein Pept. Sci. Kuznetsov 10 607 2009 10.2174/138920309789630552
Proteins: Struct., Funct., Bioinf. Gohlke 56 322 2004 10.1002/prot.20116
BMC Bioinf. Craig 14 1 2013 10.1186/1471-2105-14-S19-S1
PLoS One Yin 10 e0126864 2015 10.1371/journal.pone.0126864
J. Chem. Inf. Model. Zhang 54 2826 2014 10.1021/ci500339v
Appl. Biochem. Biotechnol. Tan 173 1752 2014 10.1007/s12010-014-0962-7
Appl. Biochem. Microbiol. Surzhik 50 118 2014 10.1134/S0003683814020185
Appl. Environ. Microbiol. Liu 80 798 2014 10.1128/AEM.03045-13
Enzyme Microb. Technol. Ding 53 365 2013 10.1016/j.enzmictec.2013.08.001
Nucleic Acids Res. Liu 34 W235 2006 10.1093/nar/gkl163
Biochemistry Kaufmann 49 2987 2010 10.1021/bi902153g
Science Korkegian 308 857 2005 10.1126/science.1107387
Nucleic Acids Res. Bava 32 D120 2004 10.1093/nar/gkh082
J. Mol. Biol. Guerois 320 369 2002 10.1016/S0022-2836(02)00442-4
BMC Bioinf. Tian 11 1 2010 10.1186/1471-2105-11-370
Bioinformatics Dehouck 25 2537 2009 10.1093/bioinformatics/btp445
Bioinformatics Huang 23 1292 2007 10.1093/bioinformatics/btm100
Open Struct. Biol. J. Huang 3 143 2009 10.2174/18741991008020100143
Bioinformatics Huang 25 2181 2009 10.1093/bioinformatics/btp370
Bioinformatics Masso 24 2002 2008 10.1093/bioinformatics/btn353
Nucleic Acids Res. Parthiban 34 W239 2006 10.1093/nar/gkl190
Proteins: Struct., Funct., Bioinf. Cheng 62 1125 2006 10.1002/prot.20810
Bioinformatics Capriotti 21 ii54 2005 10.1093/bioinformatics/bti1109
Protein Eng., Des. Sel. Kang 22 75 2009 10.1093/protein/gzn063
Proteins Thangudu 67 255 2007 10.1002/prot.21318
Nucleic Acids Res. Vinayagam 32 D200 2004 10.1093/nar/gkh026
Structure Meyer 18 1399 2010 10.1016/j.str.2010.07.013
Curr. Opin. Biotechnol. Baltzer 12 355 2001 10.1016/S0958-1669(00)00227-5
Curr. Opin. Struct. Biol. Bloom 15 447 2005 10.1016/j.sbi.2005.06.004
Curr. Opin. Chem. Biol. Bolon 6 125 2002 10.1016/S1367-5931(02)00303-4
Annu. Rev. Biophys. Biomol. Struct. Butterfoss 35 49 2006 10.1146/annurev.biophys.35.040405.102046
Curr. Opin. Biotechnol. Lehmann 12 371 2001 10.1016/S0958-1669(00)00229-9
Curr. Opin. Biotechnol. van den Burg 13 333 2002 10.1016/S0958-1669(02)00325-7
Curr. Opin. Struct. Biol. Sunyaev 11 125 2001 10.1016/S0959-440X(00)00175-5
Bioinformatics Capriotti 20 1 i63 2004 10.1093/bioinformatics/bth928
Proteins Pitera 41 385 2000 10.1002/1097-0134(20001115)41:3<385::AID-PROT100>3.0.CO;2-R
Bioinformatics Deutsch 23 3009 2007 10.1093/bioinformatics/btm481
PLoS One Li 7 e47247 2012 10.1371/journal.pone.0047247
Protein Eng. Gilis 13 849 2000 10.1093/protein/13.12.849
Nucleic Acids Res. Magyar 33 W303 2005 10.1093/nar/gki409
Protein Sci. Zhou 11 2714 2002 10.1110/ps.0217002
Proteins Zhou 54 315 2004 10.1002/prot.10584
J. Mol. Biol. Guerois 320 369 2002 10.1016/S0022-2836(02)00442-4
Nucleic Acids Res. Parthiban 34 W239 2006 10.1093/nar/gkl190
BMC Bioinf. Capriotti 9 2 S6 2008 10.1186/1471-2105-9-S2-S6
Proteins Cheng 62 1125 2006 10.1002/prot.20810
Bioinformatics Dosztanyi 19 899 2003 10.1093/bioinformatics/btg110
Protein Eng., Des. Sel. Shen 21 37 2008 10.1093/protein/gzm084
Protein Eng., Des. Sel. Potapov 22 553 2009 10.1093/protein/gzp030
Comput. Biol. Chem. Dorn 53 251 2014 10.1016/j.compbiolchem.2014.10.001
Nucleic Acids Res. de Brevern 40 W317 2012 10.1093/nar/gks482
J. Biomol. Struct. Dyn. OmPraba 25 311 2007 10.1080/07391102.2007.10507179
Protein Eng. Manco 13 197 2000 10.1093/protein/13.3.197
J. Appl. Sci. Environ. Sanit. Singh 6 485 2011
Molecular Modeling of Thermostable Endoglucanases Wong 2007 J. Wong , Molecular Modeling of Thermostable Endoglucanases, ProQuest, 2007
Biologia Gontia-Mishra 69 1283 2014 10.2478/s11756-014-0447-8
J. Mol. Microbiol. Biotechnol. Farrokh 24 262 2014 10.1159/000365890
Proc. Natl. Acad. Sci. U. S. A. Wang 110 7619 2013 10.1073/pnas.1300233110
Nucleic Acids Res. Biasini gku340 2014
Current Protocols in Bioinformatics Webb 5.6.1 2014 10.1002/0471250953.bi0506s47
Enzyme Microb. Technol. Feng 84 78 2016 10.1016/j.enzmictec.2015.12.002
Biotechnol. Lett. Kaneko 27 1777 2005 10.1007/s10529-005-3555-2
Bioresour. Technol. Mabrouk 102 1740 2011 10.1016/j.biortech.2010.08.082
Appl. Biochem. Biotechnol. Mu 176 1736 2015 10.1007/s12010-015-1675-2
Photochem. Photobiol. Sci. Alipour 8 847 2009 10.1039/b901938c
Adv. Genet. Eng. Rakesh 2015 2015 2169-0111.1000126
J. Biotechnol. Akbulut 164 123 2013 10.1016/j.jbiotec.2012.12.016
Evol. Bioinf. Kumwenda 9 327 2013 10.4137/EBO.S12539
Biochem. Biophys. Res. Commun. Sinchaikul 283 868 2001 10.1006/bbrc.2001.4854
Appl. Environ. Microbiol. Lee 72 1588 2006 10.1128/AEM.72.2.1588-1594.2006
Chin. J. Chem. Eng. Xiaoyan 20 52 2012 10.1016/S1004-9541(12)60363-2
Appl. Biochem. Biotechnol. Wang 164 1323 2011 10.1007/s12010-011-9215-1
Proteins: Struct., Funct., Bioinf. Sun 83 485 2015 10.1002/prot.24744
Bioinformatics Andreani btv041 2015
Bioinformatics Di Lena 28 2449 2012 10.1093/bioinformatics/bts475
Biomicrofluidics Brown 9 054124 2015 10.1063/1.4934713
Elife Hopf 3 e03430 2014 10.7554/eLife.03430
Bioinformatics Galzitskaya 22 2948 2006 10.1093/bioinformatics/btl504
Bioinformatics Schlessinger 22 891 2006 10.1093/bioinformatics/btl032
Nucleic Acids Res. Cilia 42 W264 2014 10.1093/nar/gku270
BMC Bioinf. Kountouris 10 1 2009 10.1186/1471-2105-10-437
J. Comput. Biol. Borguesan 2016 10.1089/cmb.2016.0074
Nucleic Acids Res. Drozdetskiy gkv332 2015
Nucleic Acids Res. Ferrè 34 W182 2006 10.1093/nar/gkl189
Bioinformatics Yang 31 3773 2015 10.1093/bioinformatics/btv459
J. Parallel Distr. Comput. Yaseen 72 2 297 2012 10.1016/j.jpdc.2011.10.005
Nucleic Acids Res. Ceroni 34 W177 2006 10.1093/nar/gkl266
How protein stability and new functions trade off, PLoS Comput. Biol. Tokuriki 4 2 e1000002 2008
Structure and mechanism in protein science: a guide to enzyme catalysis and protein folding Fersht 1999 A. Fersht , Structure and mechanism in protein science: a guide to enzyme catalysis and protein folding, W. H. Freeman, New York, 1999
Protein Eng. Ollis 5 197 1992 10.1093/protein/5.3.197
J. Mol. Biol. Beadle 321 285 2002 10.1016/S0022-2836(02)00599-5
Biochemistry Garcia 39 11227 2000 10.1021/bi0010266
Biochemistry Nagatani 46 6688 2007 10.1021/bi700507d
J. Mol. Biol. Wang 320 85 2002 10.1016/S0022-2836(02)00400-X
J. Am. Chem. Soc. Chen 127 5423 2005 10.1021/ja042850a
Proc. Natl. Acad. Sci. U. S. A. Bloom 103 5869 2006 10.1073/pnas.0510098103
J. Mol. Biol. Godoy-Ruiz 336 313 2004 10.1016/j.jmb.2003.12.048
Protein Eng. Zhao 12 47 1999 10.1093/protein/12.1.47
Arch. Biochem. Biophys. Manco 373 182 2000 10.1006/abbi.1999.1497
Biochemistry Gershenson 39 4658 2000 10.1021/bi992473s
Protein Sci. Lazaridis 6 2589 1997 10.1002/pro.5560061211
Proc. Natl. Acad. Sci. U. S. A. Hernández 97 3166 2000 10.1073/pnas.97.7.3166
J. Mol. Biol. Merz 288 753 1999 10.1006/jmbi.1999.2709
Protein Adapt. Extremophiles Daniel 1 2008
J. Phys.: Condens. Matter Feller 22 323101 2010
Annu. Rev. Biochem. Siddiqui 75 403 2006 10.1146/annurev.biochem.75.103004.142723
Crit. Rev. Biotechnol. Siddiqui 1 2016
Proc. Natl. Acad. Sci. U. S. A. Low 70 430 1973 10.1073/pnas.70.2.430
Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol. Lonhienne 1543 1 2000 10.1016/S0167-4838(00)00210-7
Biotechnol. Biofuels You 9 124 2016 10.1186/s13068-016-0544-8
Appl. Environ. Microbiol. Duan 79 4072 2013 10.1128/AEM.00457-13
Sci. Rep. Liu 6 24117 2016 10.1038/srep24117
Biotechnol. Adv. Szlachcic 29 436 2011 10.1016/j.biotechadv.2011.03.005
Curr. Opin. Struct. Biol. Lazar 13 513 2003 10.1016/S0959-440X(03)00104-0
Drug Discovery Today Marshall 8 212 2003 10.1016/S1359-6446(03)02610-2
BMC Struct. Biol. Özen 9 1 2009 10.1186/1472-6807-9-66
Nucleic Acids Res. Worth 39 W215 2011 10.1093/nar/gkr363
Bioinformatics Pires 30 335 2014 10.1093/bioinformatics/btt691
Nucleic Acids Res. Pires gku411 2014
BMC Bioinf. Chen 14 1 2013 10.1186/1471-2105-14-S18-S1
Bioinformatics Fariselli 31 2816 2015 10.1093/bioinformatics/btv291
BMC Genomics Giollo 15 1 2014 10.1186/1471-2164-15-S4-S7
Nucleic Acids Res. Frappier gkv343 2015
J. Mol. Biol. Folkman 428 1394 2016 10.1016/j.jmb.2016.01.012
Bioinformatics Laimer btv769 2016
Bioinformatics Quan btw361 2016
Drug Discovery Today Hwang 5 e43 2008 10.1016/j.ddtec.2008.11.004
Curr. Opin. Biotechnol. Kontermann 22 868 2011 10.1016/j.copbio.2011.06.012
Nat. Rev. Drug Discovery Frokjaer 4 298 2005 10.1038/nrd1695
Adv. Drug Delivery Rev. Alpar 57 411 2005 10.1016/j.addr.2004.09.004
J. Controlled Release Hussain 94 15 2004 10.1016/j.jconrel.2003.10.001
Biotechnol. Prog. Rathore 24 504 2008 10.1021/bp070462h
Int. J. Pharm. Wang 185 129 1999 10.1016/S0378-5173(99)00152-0
J. Pharm. Sci. Wang 96 1 2007 10.1002/jps.20727
Nat. Struct. Mol. Biol. Malakauskas 5 470 1998 10.1038/nsb0698-470
Protein Sci. Filikov 11 1452 2002 10.1110/ps.3500102
Protein Sci. Luo 11 1218 2002 10.1110/ps.4580102
J. Mol. Biol. Zakrzewska 352 860 2005 10.1016/j.jmb.2005.07.066
Chemistry Shirley 264 11621 1989
Curr. Opin. Chem. Biol. Caravella 14 520 2010 10.1016/j.cbpa.2010.06.175
Making and Using Antibodies: A Practical Handbook Almagro 395 2013 10.1201/b15103-16 J. C. Almagro , S.Kodangattil and J.Li, Making and Using Antibodies: A Practical Handbook, 2013, p. 395
J. Mol. Biol. Bernett 396 1474 2010 10.1016/j.jmb.2009.12.046
Protein Eng., Des. Sel. Kügler 22 135 2009 10.1093/protein/gzn079
Protein Eng., Des. Sel. Honegger 22 121 2009 10.1093/protein/gzn077
J. Pharm. Sci. Fishburn 97 4167 2008 10.1002/jps.21278
Biotechnol. J. Jevševar 5 113 2010 10.1002/biot.200900218
Proteins: Struct., Funct., Bioinf. Wang 76 99 2009 10.1002/prot.22319
J. Biol. Chem. Borras 285 9054 2010 10.1074/jbc.M109.072876
Curr. Opin. Chem. Biol. Gebauer 13 245 2009 10.1016/j.cbpa.2009.04.627
J. Mol. Biol. Saerens 377 478 2008 10.1016/j.jmb.2008.01.022
J. Biol. Chem. Gong 284 14203 2009 10.1074/jbc.M900769200
Biochemistry Culajay 39 7153 2000 10.1021/bi9927742
J. Protein Chem. Arakawa 12 525 1993 10.1007/BF01025117
Jpn. J. Clin. Oncol. Ishikawa 21 169 1991
Proc. Natl. Acad. Sci. U. S. A. Mark 81 5662 1984 10.1073/pnas.81.18.5662
J. Mol. Biol. Wang 380 623 2008 10.1016/j.jmb.2008.05.025
Proc. Natl. Acad. Sci. U. S. A. Pipe 94 11851 1997 10.1073/pnas.94.22.11851
*원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다.
Copyright KISTI. All Rights Reserved.
※ AI-Helper는 부적절한 답변을 할 수 있습니다.