Print page    

Publications

Preferences: 
References per page: Year: Medium:

  
Show abstracts

Articles (1):

41. Ferris H U , Dunin-Horkawicz S , Hornig N , Hulko M , Martin J , Schultz J E , Zeth K , Lupas A N and Coles M (2012) Mechanism of regulation of receptor histidine kinases Structure 20(1) 56-66.
CiteID: FerrisDHHMSZLC2012
40. Ferris H U , Dunin-Horkawicz S , Mondejar L G , Hulko M , Hantke K , Martin J , Schultz J E , Zeth K , Lupas A N and Coles M (2011) The mechanisms of HAMP-mediated signaling in transmembrane receptors Structure 19(3) 378-85.
CiteID: FerrisDMHHMSZLC2011
39. Alvarez B H , Gruber M , Ursinus A , Dunin-Horkawicz S , Lupas A N and Zeth K (2010) A transition from strong right-handed to canonical left-handed supercoiling in a conserved coiled-coil segment of trimeric autotransporter adhesins J Struct Biol 170(2) 236-45.
CiteID: AlvarezGUDLZ2010
38. Djuranovic S , Hartmann M D , Habeck M , Ursinus A , Zwickl P , Martin J , Lupas A N and Zeth K (2009) Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases Mol Cell 34(5) 580-90.
CiteID: DjuranovicHHUZMLZ2009
37. Serek-Heuberger J , Hobel C F , Dunin-Horkawicz S , Rockel B , Martin J and Lupas A N (2009) Two unique membrane-bound AAA proteins from Sulfolobus solfataricus Biochem Soc Trans 37(Pt 1) 118-22.
CiteID: SerekHeubergerHDRML2009
36. Szczesny P , Linke D , Ursinus A , Bar K , Schwarz H , Riess T M , Kempf V A , Lupas A N , Martin J and Zeth K (2008) Structure of the head of the Bartonella adhesin BadA PLoS Pathog 4(8) e1000119.
CiteID: SzczesnyLUBSRKLMZ2008
35. Hulko M , Lupas A N and Martin J (2007) Inherent chaperone-like activity of aspartic proteases reveals a distant evolutionary relation to double-psi barrel domains of AAA-ATPases Protein Sci 16(4) 644-53.
CiteID: HulkoLM2007
34. Ahituv N , Kavaslar N , Schackwitz W , Ustaszewska A , Martin J , Hebert S , Doelle H , Ersoy B , Kryukov G , Schmidt S , Yosef N , Ruppin E , Sharan R , Vaisse C , Sunyaev S , Dent R , Cohen J , McPherson R and Pennacchio L A (2007) Medical sequencing at the extremes of human body mass Am J Hum Genet 80(4) 779-91.
CiteID: AhituvKSUMHDEKSYRSVSDCMP2007
33. Schmidt O , Schuenemann V J , Hand N J , Silhavy T J , Martin J , Lupas A N and Djuranovic S (2007) prlF and yhaV encode a new toxin-antitoxin system in Escherichia coli J Mol Biol 372(4) 894-905.
CiteID: SchmidtSHSMLD2007
32. Djuranovic S , Rockel B , Lupas A N and Martin J (2006) Characterization of AMA, a new AAA protein from Archaeoglobus and methanogenic archaea J Struct Biol 156(1) 130-8.
CiteID: DjuranovicRLM2006
31. Riess T , Andersson S G , Lupas A , Schaller M , Schafer A , Kyme P , Martin J , Walzlein J H , Ehehalt U , Lindroos H , Schirle M , Nordheim A , Autenrieth I B and Kempf V A (2004) Bartonella adhesin a mediates a proangiogenic host cell response J Exp Med 200(10) 1267-78.
CiteID: RiessALSSKMWELSNAK2004
30. Martin J (2004) Chaperonin function--effects of crowding and confinement J Mol Recognit 17(5) 465-72.
CiteID: Martin2004
29. Martin J , Gruber M and Lupas A N (2004) Coiled coils meet the chaperone world Trends Biochem Sci 29(9) 455-8.
CiteID: MartinGL2004
28. Kusmierczyk A R and Martin J (2003) Nested cooperativity and salt dependence of the ATPase activity of the archaeal chaperonin Mm-cpn FEBS Lett 547(1-3) 201-4.
CiteID: KusmierczykM2003
27. Kusmierczyk A R and Martin J (2003) Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis Biochem J 371(Pt 3) 669-73.
CiteID: KusmierczykM2003_2
26. Lupas A N and Martin J (2002) AAA proteins Curr Opin Struct Biol 12(6) 746-53.
CiteID: LupasM2002
25. Martin J (2002) Requirement for GroEL/GroES-dependent protein folding under nonpermissive conditions of macromolecular crowding Biochemistry 41(15) 5050-5.
CiteID: Martin2002
24. Kusmierczyk A R and Martin J (2001) Assembly of chaperonin complexes Mol Biotechnol 19(2) 141-52.
CiteID: KusmierczykM2001
23. Kusmierczyk A R and Martin J (2001) Chaperonins--keeping a lid on folding proteins FEBS Lett 505(3) 343-7.
CiteID: KusmierczykM2001_2
22. Kusmierczyk A R and Martin J (2000) High salt-induced conversion of Escherichia coli GroEL into a fully functional thermophilic chaperonin J Biol Chem 275(43) 33504-11.
CiteID: KusmierczykM2000
21. Martin J (1998) Protein folding assisted by the GroEL/GroES chaperonin system Biochemistry (Mosc) 63(4) 374-81.
CiteID: Martin1998
20. Martin J (1998) Role of the GroEL chaperonin intermediate domain in coupling ATP hydrolysis to polypeptide release J Biol Chem 273(13) 7351-7.
CiteID: Martin1998_2
19. Martin J and Hartl F U (1997) Chaperone-assisted protein folding Curr Opin Struct Biol 7(1) 41-52.
CiteID: MartinH1997_2
18. Martin J and Hartl F U (1997) The effect of macromolecular crowding on chaperonin-mediated protein folding Proc Natl Acad Sci U S A 94(4) 1107-12.
CiteID: MartinH1997
17. Mayhew M , da Silva A C , Martin J , Erdjument-Bromage H , Tempst P and Hartl F U (1996) Protein folding in the central cavity of the GroEL-GroES chaperonin complex Nature 379(6564) 420-6.
CiteID: MayhewdMETH1996
16. Hayer-Hartl M K , Martin J and Hartl F U (1995) Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding Science 269(5225) 836-41.
CiteID: HayerHartlMH1995
15. Hartl F U and Martin J (1995) Molecular chaperones in cellular protein folding Curr Opin Struct Biol 5(1) 92-102.
CiteID: HartlM1995
14. Martin J and Hartl F U (1994) Molecular chaperones in cellular protein folding Bioessays 16(9) 689-92.
CiteID: MartinH1994
13. Martin J , Goldie K N , Engel A and Hartl F U (1994) Topology of the morphological domains of the chaperonin GroEL visualized by immuno-electron microscopy Biol Chem Hoppe Seyler 375(9) 635-9.
CiteID: MartinGEH1994
12. Martin J , Geromanos S , Tempst P and Hartl F U (1993) Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES Nature 366(6452) 279-82.
CiteID: MartinGTH1993
11. Martin J and Hartl F U (1993) Protein folding in the cell: molecular chaperones pave the way Structure 1(3) 161-4.
CiteID: MartinH1993
10. Martin J , Mayhew M , Langer T and Hartl F U (1993) The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding Nature 366(6452) 228-33.
CiteID: MartinMLH1993
9. Langer T , Pfeifer G , Martin J , Baumeister W and Hartl F U (1992) Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity EMBO J 11(13) 4757-65.
CiteID: LangerPMBH1992
8. Ackerman S H , Martin J and Tzagoloff A (1992) Characterization of ATP11 and detection of the encoded protein in mitochondria of Saccharomyces cerevisiae J Biol Chem 267(11) 7386-94.
CiteID: AckermanMT1992
7. Martin J , Horwich A L and Hartl F U (1992) Prevention of protein denaturation under heat stress by the chaperonin Hsp60 Science 258(5084) 995-8.
CiteID: MartinHH1992
6. Hartl F U , Martin J and Neupert W (1992) Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60 Annu Rev Biophys Biomol Struct 21 293-322.
CiteID: HartlMN1992
5. West A H , Clark D J , Martin J , Neupert W , Hartl F U and Horwich A L (1992) Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein J Biol Chem 267(34) 24625-33.
CiteID: WestCMNHH1992
4. Martin J , Langer T , Boteva R , Schramel A , Horwich A L and Hartl F U (1991) Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate Nature 352(6330) 36-42.
CiteID: MartinLBSHH1991
3. Martin J , Mahlke K and Pfanner N (1991) Role of an energized inner membrane in mitochondrial protein import. Delta psi drives the movement of presequences J Biol Chem 266(27) 18051-7.
CiteID: MartinMP1991
2. Mahlke K , Pfanner N , Martin J , Horwich A L , Hartl F U and Neupert W (1990) Sorting pathways of mitochondrial inner membrane proteins Eur J Biochem 192(2) 551-5.
CiteID: MahlkePMHHN1990
1. Cheng M Y , Hartl F U , Martin J , Pollock R A , Kalousek F , Neupert W , Hallberg E M , Hallberg R L and Horwich A L (1989) Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria Nature 337(6208) 620-5.
CiteID: ChengHMPKNHHH1989

Export as:
BibTeX, XML