UBIQUITIN

References

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References

Biological

Functions

Ubiquitilation

Structure

[1] Vijay-Kumar S, Bugg CE, Cook WJ. 

 Structure of ubiquitin refined at 1.8 A resolution.

J Mol Biol. 1987 Apr 5;194(3):531-44; MEDLINE

 

[2] Ramage R, Green J, Muir TW, Ogunjobi OM, Love S, Shaw K. 

 Synthetic, structural and biological studies of the ubiquitin system: the total chemical synthesis of ubiquitin.

Biochem J. 1994 Apr 1;299 ( Pt 1):151-8; MEDLINE

 

[3] Goldstein G, Scheid M, Hammerling U, Schlesinger DH, Niall HD, Boyse EA. 

 Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells.

Proc Natl Acad Sci U S A. 1975 Jan;72(1):11-5; MEDLINE

 

[4] Hunt LT, Dayhoff MO. 

 Amino-terminal sequence identity of ubiquitin and the nonhistone component of nuclear protein A24.

Biochem Biophys Res Commun. 1977 Jan 24;74(2):650-5; MEDLINE

 

[5] Goldknopf IL, Busch H. 

 Isopeptide linkage between nonhistone and histone 2A polypeptides of chromosomal conjugate-protein A24.

Proc Natl Acad Sci U S A. 1977 Mar;74(3):864-8; MEDLINE

 

[6] Etlinger JD, Goldberg AL.  

 A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes.

Proc Natl Acad Sci U S A. 1977 Jan;74(1):54-8; MEDLINE

 

[7] Ciechanover A, Heller H, Elias S, Haas AL, Hershko A.

 ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation.

Proc Natl Acad Sci U S A. 1980 Mar;77(3):1365-8; MEDLINE

 

[8] Wilkinson KD, Urban MK, Haas AL. 

 Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes.

J Biol Chem. 1980 Aug 25;255(16):7529-32; MEDLINE

 

[9] Weber PL, Brown SC, Mueller L.  

 Sequential 1H NMR assignments and secondary structure identification of human ubiquitin.

Biochemistry. 1987 Nov 17;26(23):7282-90; MEDLINE

 

[10] Di Stefano DL, Wand AJ. 

 Two-dimensional 1H NMR study of human ubiquitin: a main chain directed assignment and structure analysis.

Biochemistry. 1987 Nov 17;26(23):7272-81; MEDLINE

 

[11] Ibarra-Molero B, Loladze VV, Makhatadze GI, Sanchez-Ruiz JM. 

 Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability.

Biochemistry. 1999 Jun 22;38(25):8138-49; MEDLINE

 

[12] Ibarra-Molero B, Makhatadze GI, Sanchez-Ruiz JM. 

 Cold denaturation of ubiquitin.

Biochim Biophys Acta. 1999 Jan 11;1429(2):384-90; MEDLINE

 

[13] Wintrode PL, Makhatadze GI, Privalov PL. 

 Thermodynamics of ubiquitin unfolding.

Proteins. 1994 Mar;18(3):246-53; MEDLINE

 

[14] Stockman BJ, Euvrard A, Scahill TA. 

 Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: the A-state of human ubiquitin.

J Biomol NMR. 1993 May;3(3):285-96; MEDLINE

 

[15] Cox JP, Evans PA, Packman LC, Williams DH, Woolfson DN. 

 Dissecting the structure of a partially folded protein. Circular dichroism and nuclear magnetic resonance studies of peptides from ubiquitin.

J Mol Biol. 1993 Nov 20;234(2):483-92; MEDLINE

 

[16] Zerella R, Evans PA, Ionides JM, Packman LC, Trotter BW, Mackay JP, Williams DH. 

 Autonomous folding of a peptide corresponding to the N-terminal beta-hairpin from ubiquitin.

Protein Sci. 1999 Jun;8(6):1320-31; MEDLINE

 

[17] Jourdan M, Searle MS.  

 Cooperative assembly of a nativelike ubiquitin structure through peptide fragment complexation: energetics of peptide association and folding.

Biochemistry. 2000 Oct 10;39(40):12355-64; MEDLINE

 

[18] Briggs MS, Roder H.

 Early hydrogen-bonding events in the folding reaction of ubiquitin.

Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2017-21; MEDLINE

 

[19] Mizerski W. Tablice chemiczne. Wydawnictwo Admantan (1997) Warszawa;

 

[20] Mizerski W. Tablice biologiczne. Wydawnictwo Adamantan (1994) Warszawa;

 

[21] Bachmair A, Finley D, Varshavsky A. 

 In vivo half-life of a protein is a function of its amino-terminal residue.

Science. 1986 Oct 10;234(4773):179-86; MEDLINE

 

[22] Bachmair A, Varshavsky A.  

 The degradation signal in a short-lived protein.

Cell. 1989 Mar 24;56(6):1019-32; MEDLINE

 

[23] Hershko A. 

 Ubiquitin: roles in protein modification and breakdown.

Cell. 1983 Aug;34(1):11-2. Review; MEDLINE

 

[24] Ferguson DL. Guikema JA. Paulsen GM.

 Ubiquitine pool modulation and protein degradation In wheat roots during high temperature stress.

Plant Physiol. 1990 92 740-746;

 

[25] Haas AL, Ahrens P, Bright PM, Ankel H. 

 Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin.

J Biol Chem. 1987 Aug 15;262(23):11315-23; MEDLINE

 

[26] Manetto V, Abdul-Karim FW, Perry G, Tabaton M, Autilio-Gambetti L, Gambetti P.  

 Selective presence of ubiquitin in intracellular inclusions.

Am J Pathol. 1989 Mar;134(3):505-13; MEDLINE

 

[27] Ozkaynak E, Finley D, Solomon MJ, Varshavsky A.  

 The yeast ubiquitin genes: a family of natural gene fusions.

EMBO J. 1987 May;6(5):1429-39; MEDLINE

 

[28] Zhaung ZP, McCauley R.  

 Ubiquitin is involved in the in vitro insertion of monoamine oxidase B into mitochondrial outer membranes.

J Biol Chem. 1989 Sep 5;264(25):14594-6; MEDLINE

 

[29] Szewczuk Z, Stefanowicz P, Wilczynski A, Staszewska A, Siemion IZ, Zimecki M, Wieczorek Z.  

 Immunosuppressory activity of ubiquitin fragments containing retro-RGD sequence.

Biopolymers. 2004 Aug 5;74(5):352-62; MEDLINE

 

[30] Schlesinger DH, Goldstein G, Niall HD.  

 The complete amino acid sequence of ubiquitin, an adenylate cyclase stimulating polypeptide probably universal in living cells.

Biochemistry. 1975 May 20;14(10):2214-8; MEDLINE

 

[31] Mori H, Kondo J, Ihara Y.  

 Ubiquitin is a component of paired helical filaments in Alzheimer's disease.

Science. 1987 Mar 27;235(4796):1641-4; MEDLINE

 

[32] http://www.vli-research.com/Products_and_Solutions/NMR_Standards/Human_Ubiquitin/Properties_and_Analysis.php;

 

[33] Protein Data Bank;

 

[34] http://bioinfo.weizmann.ac.il/cards-bin/carddisp?UBB;

 

[35] http://www.nottingham.ac.uk/biochemcourses/students/ub/ubimage.html;

 

[36] Khorasanizadeh S, Peters ID, Butt TR, Roder H. 

 Folding and stability of a tryptophan-containing mutant of ubiquitin.

Biochemistry. 1993 Jul 13;32(27):7054-63; MEDLINE

 

[37] Kłyszejko-Stefanowicz L. Cytobiochemia, PWN (2002) Warszawa;

 

[38] http://homepages.bw.edu/~mbumbuli/cell/ublec/;

 

[39] http://boneslab.bio.ntnu.no/pdf/CellularDisposalProtDegraProteasome2003.pdf;

 

[40] http://www.food.rdg.ac.uk/online/fs916/lect1/lect1.htm;

 

[41] Haas AL, Warms JV, Hershko A, Rose IA.  

 Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation.

J Biol Chem. 1982 Mar 10;257(5):2543-8; MEDLINE

 

[42] Baboshina OV, Haas AL.

 Novel multiubiquitin chain linkages catalyzed by the conjugating enzymes E2EPF and RAD6 are recognized by 26 S proteasome subunit 5.

J Biol Chem. 1996 Feb 2;271(5):2823-31; MEDLINE

 

[43] Davis DL, Soldin SJ.  

 Identification of ubiquitin as an immunophilin.

Biochem Biophys Res Commun. 2000 Oct 22;277(2):325-9; MEDLINE

 

[44] Jaremko L, Jaremko M.

 Design and synthesis of two new immunosuppressants.

15th European Union Contest for Young Scientists. 2003, Budapest, Hungary; Abstract, Awards.

 

 

Aknowledgements:

 

           Authors would like to thank prof. Jacek Gliński, the vice-dean of Faculty of Chemistry of Wrocław University for a web-space on the Faculty’s server.

           The special thanks are due to our supervisors prof. Zbigniew Szewczuk, dr. Piotr Stefanowicz and dr. Alicja Kluczyk for their support and fruitful discussions.

          

 

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