메뉴 건너뛰기




Volumn 21, Issue 1, 2008, Pages 20-29

Homology versus analogy: Possible evolutionary relationship of immunoglobulins, cupredoxins, and Cu,Zn-superoxide dismutase

Author keywords

Convergent evolution; Divergent evolution; Immunoglobulin like fold; Pre biotic

Indexed keywords


EID: 39749177612     PISSN: 09523499     EISSN: 10991352     Source Type: Journal    
DOI: 10.1002/jmr.861     Document Type: Article
Times cited : (8)

References (79)
  • 1
    • 0026411154 scopus 로고
    • Copper protein structures
    • Adman ET. 1991. Copper protein structures. Adv. Protein Chem. 42: 145–197.
    • (1991) Adv. Protein Chem. , vol.42 , pp. 145-197
    • Adman, ET1
  • 2
    • 0031793928 scopus 로고    scopus 로고
    • Iterated profile searches with PSI‐BLAST—a tool for discovery in protein databases
    • Altschul SF, Koonin EV. 1998. Iterated profile searches with PSI‐BLAST—a tool for discovery in protein databases. Trends Biochem. Sci. 23: 444–447.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 444-447
    • Altschul, SF1    Koonin, EV2
  • 4
    • 0033574503 scopus 로고    scopus 로고
    • Gleaning non‐trivial structural, functional and evolutionary information about proteins by iterative database searches
    • Aravind L, Koonin EV. 1999. Gleaning non‐trivial structural, functional and evolutionary information about proteins by iterative database searches. J. Mol. Biol. 287: 1023–1040.
    • (1999) J. Mol. Biol. , vol.287 , pp. 1023-1040
    • Aravind, L1    Koonin, EV2
  • 6
    • 0029838142 scopus 로고    scopus 로고
    • Members of the immunoglobulin superfamily in bacteria
    • Bateman A, Eddy SR, Chothia C. 1996. Members of the immunoglobulin superfamily in bacteria. Protein Sci. 5: 1939–1941.
    • (1996) Protein Sci. , vol.5 , pp. 1939-1941
    • Bateman, A1    Eddy, SR2    Chothia, C3
  • 7
    • 0030761567 scopus 로고    scopus 로고
    • A member of the immunoglobulin superfamily in bacteriophage T4
    • Bateman A, Eddy SR, Mesyanzhinov VV. 1997. A member of the immunoglobulin superfamily in bacteriophage T4. Virus Genes 14: 163–165.
    • (1997) Virus Genes , vol.14 , pp. 163-165
    • Bateman, A1    Eddy, SR2    Mesyanzhinov, VV3
  • 8
    • 0028172534 scopus 로고
    • The immunoglobulin fold: Structural classification, sequence patterns and common core
    • Bork P, Holm L, Sander C. 1994. The immunoglobulin fold: Structural classification, sequence patterns and common core. J. Mol. Biol. 242: 309–320.
    • (1994) J. Mol. Biol. , vol.242 , pp. 309-320
    • Bork, P1    Holm, L2    Sander, C3
  • 9
    • 0026740292 scopus 로고
    • Molecular cloning of CSF‐1 receptor from rat myoblasts. Sequence analysis and regulation during myogenesis
    • Borycki AG, Guillier M, Leibovitch MP, Leibovitch SA. 1992. Molecular cloning of CSF‐1 receptor from rat myoblasts. Sequence analysis and regulation during myogenesis. Growth Factors 6: 209–218.
    • (1992) Growth Factors , vol.6 , pp. 209-218
    • Borycki, AG1    Guillier, M2    Leibovitch, MP3    Leibovitch, SA4
  • 10
    • 0032568596 scopus 로고    scopus 로고
    • Assessing sequence comparison methods with reliable structurally identified distant evolutionary relationships
    • Brenner SE, Chothia C, Hubbard TJ. 1998. Assessing sequence comparison methods with reliable structurally identified distant evolutionary relationships. Proc. Natl. Acad. Sci. U.S.A. 95: 6073–6078.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6073-6078
    • Brenner, SE1    Chothia, C2    Hubbard, TJ3
  • 11
    • 0036005911 scopus 로고    scopus 로고
    • Gene 3D: structural assignment for whole genes and genomes using the CATH domain structure database
    • Buchan DWA, Shepherd AJ, Lee D, Pearle FMG, Rison SCG, Thornton JM, Orengo CA. 2002. Gene 3D: structural assignment for whole genes and genomes using the CATH domain structure database. Genome Res. 12: 503–514.
    • (2002) Genome Res. , vol.12 , pp. 503-514
    • Buchan, DWA1    Shepherd, AJ2    Lee, D3    Pearle, FMG4    Rison, SCG5    Thornton, JM6    Orengo, CA7
  • 12
    • 0033555277 scopus 로고    scopus 로고
    • The structure of a PKD domain from polycystin‐1: implications for polycystic kidney disease
    • Bycroft M, Bateman A, Clarke J, Hamill SJ, Sandford R, Thomas RL, Chothia C. 1999. The structure of a PKD domain from polycystin‐1: implications for polycystic kidney disease. EMBO J. 18: 297–305.
    • (1999) EMBO J. , vol.18 , pp. 297-305
    • Bycroft, M1    Bateman, A2    Clarke, J3    Hamill, SJ4    Sandford, R5    Thomas, RL6    Chothia, C7
  • 15
    • 0035823119 scopus 로고    scopus 로고
    • Understanding hierarchical protein evolution from first principles
    • Dokholyan NV, Shakhnovich EI. 2001. Understanding hierarchical protein evolution from first principles. J. Mol. Biol. 312: 289–307.
    • (2001) J. Mol. Biol. , vol.312 , pp. 289-307
    • Dokholyan, NV1    Shakhnovich, EI2
  • 16
    • 0004089638 scopus 로고
    • Of URF's and ORF's: a primer on how to analyze derived amino acid sequences
    • Doolittle RF. 1986. Of URF's and ORF's: a primer on how to analyze derived amino acid sequences. University Science Books: Mill Valley, CA.
    • (1986)
    • Doolittle, RF1
  • 17
    • 0027983037 scopus 로고
    • Convergent evolution: the need to be explicit
    • Doolittle RF. 1994. Convergent evolution: the need to be explicit. Trends Bichem. Sci. 19: 15–18.
    • (1994) Trends Bichem. Sci. , vol.19 , pp. 15-18
    • Doolittle, RF1
  • 18
    • 0019568541 scopus 로고
    • Internal duplication and evolution of human ceruloplasmin
    • Dwulet FE, Putnam FW. 1981. Internal duplication and evolution of human ceruloplasmin. Proc. Natl. Acad. Sci. U.S.A. 78: 2805–2809.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 2805-2809
    • Dwulet, FE1    Putnam, FW2
  • 19
    • 2942544229 scopus 로고    scopus 로고
    • COACH: profile–profile alignment of protein families using hidden Markov models
    • Edgar RC, Sjolander K. 2004. COACH: profile–profile alignment of protein families using hidden Markov models. Bioinformatics 20: 1309–1318.
    • (2004) Bioinformatics , vol.20 , pp. 1309-1318
    • Edgar, RC1    Sjolander, K2
  • 20
    • 0024791087 scopus 로고
    • Three‐dimensional structure of a light chain dimer crystallized in water. Conformational flexibility of a molecule in two crystal forms
    • Ely KR, Herron JN, Harker M, Edmundson AB. 1989. Three‐dimensional structure of a light chain dimer crystallized in water. Conformational flexibility of a molecule in two crystal forms. J. Mol. Biol. 210: 601–615.
    • (1989) J. Mol. Biol. , vol.210 , pp. 601-615
    • Ely, KR1    Herron, JN2    Harker, M3    Edmundson, AB4
  • 21
    • 0016804680 scopus 로고
    • The molecular structure of a dimer composed of the variable portions of the Bence Jones protein REI refined at 2.0 A resolution
    • Epp O, Lattman EE, Schiffer M, Huber R, Palm W. 1975. The molecular structure of a dimer composed of the variable portions of the Bence Jones protein REI refined at 2.0 A resolution. Biochemistry 14: 4943–4952.
    • (1975) Biochemistry , vol.14 , pp. 4943-4952
    • Epp, O1    Lattman, EE2    Schiffer, M3    Huber, R4    Palm, W5
  • 22
    • 34249950368 scopus 로고    scopus 로고
    • Beyond host‐pathogen interactions: microbial defense strategy in the host environment
    • Fialho AM, Stevens FJ, Das Gupta TK, Chakrabartty AM. 2007. Beyond host‐pathogen interactions: microbial defense strategy in the host environment. Curr. Opin. Biotechnol. 18: 1–18.
    • (2007) Curr. Opin. Biotechnol. , vol.18 , pp. 1-18
    • Fialho, AM1    Stevens, FJ2    Das Gupta, TK3    Chakrabartty, AM4
  • 23
    • 0034178257 scopus 로고    scopus 로고
    • Homology a personal view on some of the problems
    • Fitch WM. 2000. Homology a personal view on some of the problems. Trends Genet. 16: 227–231.
    • (2000) Trends Genet. , vol.16 , pp. 227-231
    • Fitch, WM1
  • 24
    • 0018261948 scopus 로고
    • Superoxide dismutases: defence against endogenous superoxide radical
    • Fridovich I. 1978. Superoxide dismutases: defence against endogenous superoxide radical. Ciba Found. Symp. 65: 77–93.
    • (1978) Ciba Found. Symp. , vol.65 , pp. 77-93
    • Fridovich, I1
  • 25
    • 0034564505 scopus 로고    scopus 로고
    • Glimmers in the midnight zone: characterization of aligned identical residues in sequence‐dissimilar proteins sharing a common fold
    • Friedberg I, Kaplan T, Margalit H. 2000. Glimmers in the midnight zone: characterization of aligned identical residues in sequence‐dissimilar proteins sharing a common fold. Proc. Int. Conf. Intell. Syst. Mol. Evol. 8: 162–170.
    • (2000) Proc. Int. Conf. Intell. Syst. Mol. Evol. , vol.8 , pp. 162-170
    • Friedberg, I1    Kaplan, T2    Margalit, H3
  • 26
    • 0035783063 scopus 로고    scopus 로고
    • Fold change in evolution of protein structures
    • Grishin NV. 2001. Fold change in evolution of protein structures. J. Struct. Biol. 134: 167–185.
    • (2001) J. Struct. Biol. , vol.134 , pp. 167-185
    • Grishin, NV1
  • 27
    • 0034695407 scopus 로고    scopus 로고
    • Conservation of folding and stability within a protein family: the tyrosine corner as an evolutionary cul‐de‐sac
    • Hamill SJ, Cota E, Chothia C, Clarke J. 2000a. Conservation of folding and stability within a protein family: the tyrosine corner as an evolutionary cul‐de‐sac. J. Mol. Biol. 295: 641–649.
    • (2000) J. Mol. Biol. , vol.295 , pp. 641-649
    • Hamill, SJ1    Cota, E2    Chothia, C3    Clarke, J4
  • 28
    • 0034677663 scopus 로고    scopus 로고
    • The folding of an immunoglobulin‐like Greek key protein is defined by a common‐core nucleus and regions constrained by topology
    • Hamill SJ, Steward A, Clarke J. 2000b. The folding of an immunoglobulin‐like Greek key protein is defined by a common‐core nucleus and regions constrained by topology. J. Mol. Biol. 297: 165–178.
    • (2000) J. Mol. Biol. , vol.297 , pp. 165-178
    • Hamill, SJ1    Steward, A2    Clarke, J3
  • 29
    • 0028568291 scopus 로고
    • The tyrosine corner: a feature of most Greek key beta‐barrel proteins
    • Hemmingsen JM, Gernert KM, Richardson JS, Richardson DS. 1994. The tyrosine corner: a feature of most Greek key beta‐barrel proteins. Protein Sci. 3: 1927–1933.
    • (1994) Protein Sci. , vol.3 , pp. 1927-1933
    • Hemmingsen, JM1    Gernert, KM2    Richardson, JS3    Richardson, DS4
  • 30
    • 0032104511 scopus 로고    scopus 로고
    • Unification of protein families
    • Holm L. 1998. Unification of protein families. Curr. Opin. Struct. Biol. 8: 372–379.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 372-379
    • Holm, L1
  • 31
    • 0029069583 scopus 로고
    • The polycystic kidney disease 1 (PKD1) gene encodes a novel protein with multiple cell recognition domains
    • Hughes J, Ward CJ, Peral B, Aspinwall R, Clark K, San Millan JL. Gamble V, Harris PC. 1995. The polycystic kidney disease 1 (PKD1) gene encodes a novel protein with multiple cell recognition domains. Nat. Genet. 10: 151–160.
    • (1995) Nat. Genet. , vol.10 , pp. 151-160
    • Hughes, J1    Ward, CJ2    Peral, B3    Aspinwall, R4    Clark, K5    San Millan, JL6    Gamble, V7    Harris, PC8
  • 32
    • 0036081436 scopus 로고    scopus 로고
    • In search for more accurate alignments in the twilight zone
    • Jaroszewski L, Li W, Godzik A. 2002. In search for more accurate alignments in the twilight zone. Protein Sci. 11: 1702–1713.
    • (2002) Protein Sci. , vol.11 , pp. 1702-1713
    • Jaroszewski, L1    Li, W2    Godzik, A3
  • 33
    • 0042706146 scopus 로고    scopus 로고
    • Moonlighting proteins: old proteins learning new tricks
    • Jeffery CJ. 2003. Moonlighting proteins: old proteins learning new tricks. Trends Genet. 19: 415–417.
    • (2003) Trends Genet. , vol.19 , pp. 415-417
    • Jeffery, CJ1
  • 34
    • 9944225262 scopus 로고    scopus 로고
    • Molecular mechanisms for multitasking: recent crystal structures of moonlighting proteins
    • Jeffery CJ. 2004. Molecular mechanisms for multitasking: recent crystal structures of moonlighting proteins. Curr. Opin. Struct. Biol. 14: 663–668.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 663-668
    • Jeffery, CJ1
  • 35
    • 0036774262 scopus 로고    scopus 로고
    • Archaeal surface layer proteins contain beta propeller, PKD, beta helix domains and are related to metazoan cell surface proteins
    • Jing H, Takagi J, Liu JH, Lindgren S, Zhang RG, Joachimiak A, Wang JH, Springer TA. 2002. Archaeal surface layer proteins contain beta propeller, PKD, beta helix domains and are related to metazoan cell surface proteins. Structure (Camb) 10: 1453–1464.
    • (2002) Structure (Camb) , vol.10 , pp. 1453-1464
    • Jing, H1    Takagi, J2    Liu, JH3    Lindgren, S4    Zhang, RG5    Joachimiak, A6    Wang, JH7    Springer, TA8
  • 36
    • 50449161451 scopus 로고
    • Papers on chemical pathology: prefaced by the Gulstonian lectures, read at the Royal College of Physicians, 1846. Lecture III
    • Jones HB. 1847. Papers on chemical pathology: prefaced by the Gulstonian lectures, read at the Royal College of Physicians, 1846. Lecture III. Lancet 2: 88–92.
    • (1847) Lancet , vol.2 , pp. 88-92
    • Jones, HB1
  • 37
    • 0015247402 scopus 로고
    • Attempts to locate complementarity‐determining residues in the variable positions of light and heavy chains
    • Kabat EA, Wu TT. 1971. Attempts to locate complementarity‐determining residues in the variable positions of light and heavy chains. Ann. N. Y. Acad. Sci. 190: 382–393.
    • (1971) Ann. N. Y. Acad. Sci. , vol.190 , pp. 382-393
    • Kabat, EA1    Wu, TT2
  • 38
    • 0032438987 scopus 로고    scopus 로고
    • Hidden Markov models for detecting remote protein homologies
    • Karplus K, Barrett C, Hughey R. 1998. Hidden Markov models for detecting remote protein homologies. Bioinformatics 14: 846–856.
    • (1998) Bioinformatics , vol.14 , pp. 846-856
    • Karplus, K1    Barrett, C2    Hughey, R3
  • 39
    • 0014292086 scopus 로고
    • The structure of carboxypeptidase A. VII. The 2.0‐angstrom resolution studies of the enzyme and of its complex with glycyltyrosine, and mechanistic deductions
    • Lipscomb WN, Hartsuck JA, Reeke GN, Jr., Quiocho FA, Bethge PH, Ludwig ML, Steitz TA, Muirhead H, Coppola JC. 1968. The structure of carboxypeptidase A. VII. The 2.0‐angstrom resolution studies of the enzyme and of its complex with glycyltyrosine, and mechanistic deductions. Brookhaven Symp. Biol. 21: 24–90.
    • (1968) Brookhaven Symp. Biol. , vol.21 , pp. 24-90
    • Lipscomb, WN1    Hartsuck, JA2    Reeke, GN3    Quiocho, FA4    Bethge, PH5    Ludwig, ML6    Steitz, TA7    Muirhead, H8    Coppola, JC9
  • 41
    • 0033120222 scopus 로고    scopus 로고
    • Identification of homologous core structures
    • Matsuo Y, Bryant SH. 1999. Identification of homologous core structures. Proteins 35: 70–79.
    • (1999) Proteins , vol.35 , pp. 70-79
    • Matsuo, Y1    Bryant, SH2
  • 42
    • 0014935646 scopus 로고
    • Natural selection and the concept of a protein space
    • Maynard Smith J. 1970. Natural selection and the concept of a protein space. Nature 225: 563–564.
    • (1970) Nature , vol.225 , pp. 563-564
    • Maynard Smith, J1
  • 43
    • 0036384350 scopus 로고    scopus 로고
    • One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions
    • Nagano N, Orengo CA, Thornton JM. 2002. One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions. J. Mol. Biol. 321: 741–765.
    • (2002) J. Mol. Biol. , vol.321 , pp. 741-765
    • Nagano, N1    Orengo, CA2    Thornton, JM3
  • 44
    • 0028593509 scopus 로고
    • Protein superfamilies and domain superfolds
    • Orengo CA, Jones DT, Thornton JM. 1994. Protein superfamilies and domain superfolds. Nature 372: 631–634.
    • (1994) Nature , vol.372 , pp. 631-634
    • Orengo, CA1    Jones, DT2    Thornton, JM3
  • 48
    • 20444449200 scopus 로고    scopus 로고
    • The limits of protein sequence comparison?
    • Pearson WR, Sierk ML. 2005. The limits of protein sequence comparison? Curr. Opin. Struct. Biol. 15: 254–260.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 254-260
    • Pearson, WR1    Sierk, ML2
  • 49
    • 34248532415 scopus 로고    scopus 로고
    • PROMALS: towards accurate multiple sequence alignments of distantly related proteins
    • Pei J, Grishin NV. 2007. PROMALS: towards accurate multiple sequence alignments of distantly related proteins. Bioinformatics 23: 802–808.
    • (2007) Bioinformatics , vol.23 , pp. 802-808
    • Pei, J1    Grishin, NV2
  • 50
    • 0000454598 scopus 로고
    • Refinement of the structure of pseudoazurin from Alcaligenes faecalis S‐6 at 1.55 A resolution
    • Petratos K, Dauter Z, Wilson KS. 1988. Refinement of the structure of pseudoazurin from Alcaligenes faecalis S‐6 at 1.55 A resolution. Acta Crystallogr. B 44 (Pt 6): 628–636.
    • (1988) Acta Crystallogr. B , vol.44 , Issue.Pt 6 , pp. 628-636
    • Petratos, K1    Dauter, Z2    Wilson, KS3
  • 51
    • 18944397862 scopus 로고    scopus 로고
    • Template‐based recognition of protein fold within the midnight and twilight zones of protein sequence similarity
    • Pirun M, Babnigg G, Stevens FJ. 2005. Template‐based recognition of protein fold within the midnight and twilight zones of protein sequence similarity. J. Mol. Recognit. 18: 203–212.
    • (2005) J. Mol. Recognit. , vol.18 , pp. 203-212
    • Pirun, M1    Babnigg, G2    Stevens, FJ3
  • 52
    • 0015733869 scopus 로고
    • Three‐dimensional structure of the Fab' fragment of a human immunoglobulin at 2,8‐A resolution
    • Poljak RJ, Amzel LM, Avey HP, Chen BL, Phizackerley RP, Saul F. 1973. Three‐dimensional structure of the Fab' fragment of a human immunoglobulin at 2,8‐A resolution. Proc. Natl. Acad. Sci. U.S.A. 70: 3305–3310.
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.70 , pp. 3305-3310
    • Poljak, RJ1    Amzel, LM2    Avey, HP3    Chen, BL4    Phizackerley, RP5    Saul, F6
  • 53
    • 0345689559 scopus 로고    scopus 로고
    • Bacterial cupredoxin azurin and its interactions with the tumor suppressor protein p53
    • Punj V, Das Gupta TK, Chakrabarty AM. 2003. Bacterial cupredoxin azurin and its interactions with the tumor suppressor protein p53. Biochem. Biophys. Res. Commun. 312: 109–114.
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , pp. 109-114
    • Punj, V1    Das Gupta, TK2    Chakrabarty, AM3
  • 54
    • 16644387358 scopus 로고    scopus 로고
    • Microbial‐based therapy of cancer: a new twist to age old practice
    • Punj V, Saint‐Dic D, Daghfal S, Kanwar JR. 2004. Microbial‐based therapy of cancer: a new twist to age old practice. Cancer Biol. Ther. 3: 708–714.
    • (2004) Cancer Biol. Ther. , vol.3 , pp. 708-714
    • Punj, V1    Saint‐Dic, D2    Daghfal, S3    Kanwar, JR4
  • 56
    • 0001495297 scopus 로고
    • Crystal structure of bovine Cu,Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands
    • Richardson J, Thomas KA, Rubin BH, Richardson DC. 1975. Crystal structure of bovine Cu,Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands. Proc. Natl. Acad. Sci. U.S.A. 72: 1349–1353.
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 1349-1353
    • Richardson, J1    Thomas, KA2    Rubin, BH3    Richardson, DC4
  • 57
    • 84886620588 scopus 로고
    • Similarity of three‐dimensional structure between the immunoglobulin domain and the copper, zinc superoxide dismutase subunit
    • Richardson JS, Richardson DC, Thomas KA, Silverton EW, Davies DR. 1976. Similarity of three‐dimensional structure between the immunoglobulin domain and the copper, zinc superoxide dismutase subunit. J. Mol. Biol. 102: 221–235.
    • (1976) J. Mol. Biol. , vol.102 , pp. 221-235
    • Richardson, JS1    Richardson, DC2    Thomas, KA3    Silverton, EW4    Davies, DR5
  • 58
    • 0032962457 scopus 로고    scopus 로고
    • Twilight zone of protein sequence alignments
    • Rost B. 1999. Twilight zone of protein sequence alignments. Protein Eng. 12: 85–94.
    • (1999) Protein Eng. , vol.12 , pp. 85-94
    • Rost, B1
  • 60
    • 33646150915 scopus 로고    scopus 로고
    • Sequential reorganization of beta‐sheet topology by insertion of a single strand
    • Sagermann M, Baase WA, Matthews BW. 2006. Sequential reorganization of beta‐sheet topology by insertion of a single strand. Protein Sci. 15: 1085–1092.
    • (2006) Protein Sci. , vol.15 , pp. 1085-1092
    • Sagermann, M1    Baase, WA2    Matthews, BW3
  • 61
    • 0032940341 scopus 로고    scopus 로고
    • Combining sensitive database searches with multiple intermediates to detect distant homologs
    • Salamov AA, Suwa M, Orengo CA, Swindells MB. 1999. Combining sensitive database searches with multiple intermediates to detect distant homologs. Protein Eng. 12: 95–100.
    • (1999) Protein Eng. , vol.12 , pp. 95-100
    • Salamov, AA1    Suwa, M2    Orengo, CA3    Swindells, MB4
  • 63
    • 0015840644 scopus 로고
    • Structure of a lambda‐type Bence Jones protein at 3.5 A resolution
    • Schiffer M, Girling RL, Ely KR, Edmundson AB. 1973. Structure of a lambda‐type Bence Jones protein at 3.5 A resolution. Biochemistry 12: 4620–4631.
    • (1973) Biochemistry , vol.12 , pp. 4620-4631
    • Schiffer, M1    Girling, RL2    Ely, KR3    Edmundson, AB4
  • 64
    • 0031565975 scopus 로고    scopus 로고
    • Sequence profiles of immunoglobulin and immunoglobulin‐like domains
    • Smith DK, Xue H. 1997. Sequence profiles of immunoglobulin and immunoglobulin‐like domains. J. Mol. Biol. 274: 530–545.
    • (1997) J. Mol. Biol. , vol.274 , pp. 530-545
    • Smith, DK1    Xue, H2
  • 65
    • 0020059082 scopus 로고
    • Bence Jones proteins: malignant or benign?
    • Solomon A. 1982. Bence Jones proteins: malignant or benign? N. Engl. J. Med. 306: 605–607.
    • (1982) N. Engl. J. Med. , vol.306 , pp. 605-607
    • Solomon, A1
  • 66
    • 0033807726 scopus 로고    scopus 로고
    • Four structural risk factors identify most fibril‐forming kappa light chains
    • Stevens FJ. 2000. Four structural risk factors identify most fibril‐forming kappa light chains. Amyloid 7: 200–211.
    • (2000) Amyloid , vol.7 , pp. 200-211
    • Stevens, FJ1
  • 67
    • 14744301681 scopus 로고    scopus 로고
    • Efficient recognition of protein fold at low sequence identity by conservative application of Psi‐BLAST: validation
    • Stevens FJ. 2005. Efficient recognition of protein fold at low sequence identity by conservative application of Psi‐BLAST: validation. J. Mol. Recognit. 18: 139–149.
    • (2005) J. Mol. Recognit. , vol.18 , pp. 139-149
    • Stevens, FJ1
  • 68
    • 0025775997 scopus 로고
    • Bence Jones proteins: A powerful tool for fundamental study of protein chemistry and pathophysiology
    • Stevens FJ, Solomon A, Schiffer M. 1991. Bence Jones proteins: A powerful tool for fundamental study of protein chemistry and pathophysiology. Biochemistry 30: 6803–6805.
    • (1991) Biochemistry , vol.30 , pp. 6803-6805
    • Stevens, FJ1    Solomon, A2    Schiffer, M3
  • 69
    • 0034687764 scopus 로고    scopus 로고
    • Protein conformation and disease: pathological consequences of analogous mutations in homologous proteins
    • Stevens FJ, Pokkuluri PR, Schiffer M. 2000. Protein conformation and disease: pathological consequences of analogous mutations in homologous proteins. Biochemistry 39: 15291–15296.
    • (2000) Biochemistry , vol.39 , pp. 15291-15296
    • Stevens, FJ1    Pokkuluri, PR2    Schiffer, M3
  • 70
    • 33751510030 scopus 로고    scopus 로고
    • Thermodynamic aspects of immunoglobulin light chain disease, in: Conformational Diseases—A Compendium
    • Stevens FJ, Schiffer M, Argon Y. 2002. Thermodynamic aspects of immunoglobulin light chain disease. In Conformational Diseases—A Compendium, E Katchalski‐Katzir (ed.). Center for the Study of Emerging Diseases: Jerusalem ; 135–150.
    • (2002) , pp. 135-150
    • Stevens, FJ1    Schiffer, M2    Argon, Y3
  • 71
    • 14744298788 scopus 로고    scopus 로고
    • Efficient recognition of protein fold at low sequence identity by conservative application of Psi‐BLAST: application
    • Stevens FJ, Kuemmel C, Babnigg G, Collart FR. 2005. Efficient recognition of protein fold at low sequence identity by conservative application of Psi‐BLAST: application. J. Mol. Recognit. 18: 150–157.
    • (2005) J. Mol. Recognit. , vol.18 , pp. 150-157
    • Stevens, FJ1    Kuemmel, C2    Babnigg, G3    Collart, FR4
  • 72
    • 0037053429 scopus 로고    scopus 로고
    • Sequence conservation in Ig‐ like domains: the role of highly conserved proline residues in the fibronectin type III superfamily
    • Steward A, Adhya S, Clarke J. 2002. Sequence conservation in Ig‐ like domains: the role of highly conserved proline residues in the fibronectin type III superfamily. J. Mol. Biol. 318: 935–940.
    • (2002) J. Mol. Biol. , vol.318 , pp. 935-940
    • Steward, A1    Adhya, S2    Clarke, J3
  • 73
    • 0034628895 scopus 로고    scopus 로고
    • Immunoglobulin superfamily proteins in Caenorhabditis elegans
    • Teichmann SA, Chothia C. 2000. Immunoglobulin superfamily proteins in Caenorhabditis elegans. J. Mol. Biol. 296: 1367–1383.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1367-1383
    • Teichmann, SA1    Chothia, C2
  • 74
    • 0016290932 scopus 로고
    • The crystal structure of bovine Cu2+,Zn2+ superoxide dismutase at 5.5‐A resolution
    • Thomas KA, Rubin BH, Bier CJ, Richardson JS, Richardson DC. 1974. The crystal structure of bovine Cu2+,Zn2+ superoxide dismutase at 5.5‐A resolution. J. Biol. Chem. 249: 5677– 5683.
    • (1974) J. Biol. Chem. , vol.249 , pp. 5677-5683
    • Thomas, KA1    Rubin, BH2    Bier, CJ3    Richardson, JS4    Richardson, DC5
  • 76
    • 2342420462 scopus 로고    scopus 로고
    • Fold‐specific substitution matrices for protein classification
    • Vilim RB, Cunningham RM, Lu B, Kheradpour P, Stevens FJ. 2004. Fold‐specific substitution matrices for protein classification. Bioinformatics 20: 847–853.
    • (2004) Bioinformatics , vol.20 , pp. 847-853
    • Vilim, RB1    Cunningham, RM2    Lu, B3    Kheradpour, P4    Stevens, FJ5
  • 77
    • 0014828908 scopus 로고
    • An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity
    • Wu TT, Kabat EA. 1970. An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity. J. Exp. Med. 132: 211–250.
    • (1970) J. Exp. Med. , vol.132 , pp. 211-250
    • Wu, TT1    Kabat, EA2
  • 79
    • 13144281835 scopus 로고    scopus 로고
    • Regulation of mammalian cell growth and death by bacterial redox proteins: relevance to ecology and cancer therapy
    • Yamada T, Hiraoka Y, Das Gupta TK, Chakrabarty AM. 2004. Regulation of mammalian cell growth and death by bacterial redox proteins: relevance to ecology and cancer therapy. Cell Cycle 3: 752–755.
    • (2004) Cell Cycle , vol.3 , pp. 752-755
    • Yamada, T1    Hiraoka, Y2    Das Gupta, TK3    Chakrabarty, AM4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.