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3D domain swapping – implications for conformational disorders and ways of control

100%

Jaskolski M.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2011

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tom 92

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nr 1

2

Personal remarks on the future of protein crystallography and structural biology

100%

Jaskolski M.

Acta Biochimica Polonica

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2010

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tom 57

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nr 3

Protein crystallography, the main experimental method of structural biology, has undergone in the recent past three revolutionary changes leading to its unexpected renaissance. They were connected with (i) the introduction of synchrotron radiation sources for X-ray diffraction experiments, (ii) implementation of Se-Met multiwavelength anomalous diffraction (MAD) for phasing, and (iii) initiation of structural genomics (SG) programs. It can be foreseen that in the next 10-15 years protein crystallography will continue to be in this revolutionary phase. We can expect not only an; avalanche of protein crystal structures from SG centers, but also attacking of more demanding projects, such as the structure of membrane proteins and of very large macromolecular complexes. On the technological front, the introduction of X-ray radiation from free-electron lasers will revolutionize the experimental possibilities, making feasible even the imaging of single molecules and of intact biological cells.

3

Bialka PR-10 jako rezerwuar ligandow hydrofobowych w komorce roslinnej

100%

Jaskolski M.

Postępy Biologii Komórki. Suplement

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2009

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nr 25

59-68

4

3D domain swapping, protein oligomerization, and amyloid formation

100%

Jaskolski M.

Acta Biochimica Polonica

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2001

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tom 48

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nr 4

In 3D domain swapping, first described by Eisenberg, a structural element of a monomeric protein is replaced by the same element from another subunit. This process requires partial unfolding of the closed monomers that is then followed by adhesion and reconstruction of the original fold but from elements contributed by different subunits. If the interactions are reciprocal, a closed-ended dimer will be formed, but the same phenomenon has been suggested as a mechanism for the formation of open-ended polymers as well, such as those believed to exist in amyloid fibrils. There has been a rapid progress in the study of 3D domain swapping. Oligomers higher than dimers have been found, the monomer-dimer equilibrium could be controlled by mutations in the hinge element of the chain, a single protein has been shown to form more than one domain-swapped structure, and recently, the possibility of simultaneous exchange of two structural domains by a single molecule has been demonstrated. This last discovery has an important bearing on the possibility that 3D domain swapping might be indeed an amyloidogenic mechanism. Along the same lines is the discovery that a protein of proven amyloidogenic properties, human cystatin C, is capable of 3D domain swapping that leads to oligomerization. The structure of domain- swapped human cystatin C dimers explains why a naturally occurring mutant of this protein has a much higher propensity for aggregation, and also suggests how this same mechanism of 3D domain swapping could lead to an open-ended polymer that would be consistent with the cross-β structure, which is believed to be at the heart of the molecular architecture of amyloid fibrils.

5

L-Asparaginases, their friends and relation

63%

Jaskolski M., Michalska K.

Acta Biochimica Polonica

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2006

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tom 53

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nr Supplement 1

6

Structural aspects of L-asparaginases, their friends and relations

63%

Michalska K., Jaskolski M.

Acta Biochimica Polonica

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2006

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tom 53

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nr 4

7

Why a benign mutation kills enzyme activity. Structure-based analysis of the A176V mutant of Saccharomyces cerevisiae L-asparaginase I

63%

Bonthron D. T., Jaskolski M.

Acta Biochimica Polonica

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1997

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tom 44

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nr 3

A conservative and apparently harmless AI76V mutation in intracellular S. cerevisiae L-asparaginase (ScerAI) completely abolishes the enzyme activity. Sequence and structural comparisons with type II bacterial L-asparaginases show that the mutated residue is in a very conservative region and plays a vital role in the cohesion of functional tetramers of these enzymes through participation in side-chain...main-chain (Ser) Oy...O (Ala) hydrogen bonds across the tetramer interface. The fact that bacterial L-asparaginases of type I show less conservation in this region suggests that they may have different quaternary structure while adopting the subunit fold and intimate dimer architecture of type II enzymes. A comparison of all available sequences of microbial L- asparaginases confirms that separate intra- and extra-cellular enzymes evolved in prokaryotes and eukaryotes independently. However, an analysis of the available complete genome sequences reveals a surprising fact that Haemophilus influenzae possesses only a type II asparaginase while the archaebacterium Methanococcus jannaschii has a type I gene, but not a type II.

8

Sequence analysis of enzymes with asparaginase activity

63%

Borek D., Jaskolski M.

Acta Biochimica Polonica

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2001

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tom 48

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nr 4

Asparaginases catalyze the hydrolysis of asparagine to aspartic acid and ammonia. Enzymes with asparaginase activity play an important role both in the metabolism of all living organisms as well as in pharmacology. The main goal of this paper is to attempt a classification of all known enzymes with asparaginase activity, based on their amino acid sequences. Some possible phylogenetic consequences are also discussed using dendrograms and structural information derived from crystallographic studies.

9

Molecular recognition motifs in cytidinium and 2'-deoxycytidinium salts with composite anions

63%

Gilski M., Jaskolski M.

Acta Biochimica Polonica

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1998

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tom 45

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nr 4

In the crystal structures of N3-protonated cytidinium and 2'-deoxycytidinium salts with composite XYn anions capable of accepting hydrogen bonds through their Y atoms, the dominating motif of cytosinium...anion interactions consists of a pair of hydrogen bonds donated from the N3+-H protonation site and from the exoamino N4-H41 group cis to N3, and accepted by two Y centers of one anion. This multi-point recognition pattern is stable and robust and thus can be classified as a supramolecular synthon. In a broader group of N3-protonated, N1-substituted cytosinium salts with composite anions it occurs with 70% frequency. The C5 side of the cytosine ring mimics the N3+-H type synthon and shows a propensity to form an analogous motif in which a C5-H5...Y hydrogen bond replaces the strong N3+-H...Y interaction. Since the C-H...Y bond is much weaker, the secondary motif shows higher deformability and is less frequent (44%).

10

Prion diseases: a dual view of the prion hypothesis as seen from a distance

63%

Liberski P. P., Jaskolski M.

Acta Neurobiologiae Experimentalis

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2002

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tom 62

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nr 3

11

Kurt Wuthrich - co-winner of the Nobel Prize in Chemistry, 2002

63%

Jaskolski M., Liberski P. P.

Acta Neurobiologiae Experimentalis

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2002

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tom 62

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nr 4

12

Inorganic pyrophosphatase (PPase) from a higher plant

51%

Grzechowiak M., Sikorski M., Jaskolski M.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2013

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tom 94

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nr 1

13

Hyp-1 protein from St John’s wort as a PR-10 protein

51%

Sliwiak J., Dauter Z., Jaskolski M.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2013

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tom 94

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nr 1

14

Serendipitous crystallization of E. coli HPII catalase, a sequel to “the tale usually not told”

51%

Grzechowiak M., Sekula B., Jaskolski M., Ruszkowski M.

Acta Biochimica Polonica

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2021

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tom 68

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nr 1

15

Crystal structure of plant asparaginase

51%

Michalska K., Bujacz G., Jaskolski M.

Acta Biochimica Polonica

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2006

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tom 53

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nr Supplement 1

16

Crystal structure of a PR-10 nodulin in complex with trans-zeatin

51%

Ruszkowski M., Sikorski M., Jaskolski M.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2013

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tom 94

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nr 1

17

Identification of amino acid sequences via X-ray crystallography: a mini review of case studies

51%

Pietrzyk A. J., Bujacz A., Jaskolski M., Bujacz G.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2013

|

tom 94

|

nr 1

18

Odwrotna transkryptaza jako enzym odpowiedzialny za niezwykłą zmienność genetyczną ludzkiego wirusa upośledzenia odporności (HIV)

51%

Kurzynska-Kokorniak A., Jaskolski M., Figlerowicz M.

Biotechnologia

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2002

|

nr 1

19

Structural enzymology at the legume-microbe interface: S-adenosyl-L-homocysteine hydrolase of rhizobia

51%

Manszewski T., Singh K., Imiolczyk B., Jaskolski M.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2013

|

tom 94

|

nr 1

20

Professor Maciej Wiewiorowski - a man of action and a visionary 1918-2005

51%

Figlerowicz M., Markiewicz W. T., Jaskolski M.

Acta Biochimica Polonica

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2005

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tom 52

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nr 4

Ograniczanie wyników

3D domain swapping – implications for conformational disorders and ways of control

Personal remarks on the future of protein crystallography and structural biology

Bialka PR-10 jako rezerwuar ligandow hydrofobowych w komorce roslinnej

3D domain swapping, protein oligomerization, and amyloid formation

L-Asparaginases, their friends and relation

Structural aspects of L-asparaginases, their friends and relations

Why a benign mutation kills enzyme activity. Structure-based analysis of the A176V mutant of Saccharomyces cerevisiae L-asparaginase I

Sequence analysis of enzymes with asparaginase activity

Molecular recognition motifs in cytidinium and 2'-deoxycytidinium salts with composite anions

Prion diseases: a dual view of the prion hypothesis as seen from a distance

Kurt Wuthrich - co-winner of the Nobel Prize in Chemistry, 2002

Inorganic pyrophosphatase (PPase) from a higher plant

Hyp-1 protein from St John’s wort as a PR-10 protein

Serendipitous crystallization of E. coli HPII catalase, a sequel to “the tale usually not told”

Crystal structure of plant asparaginase

Crystal structure of a PR-10 nodulin in complex with trans-zeatin

Identification of amino acid sequences via X-ray crystallography: a mini review of case studies

Odwrotna transkryptaza jako enzym odpowiedzialny za niezwykłą zmienność genetyczną ludzkiego wirusa upośledzenia odporności (HIV)

Structural enzymology at the legume-microbe interface: S-adenosyl-L-homocysteine hydrolase of rhizobia

Professor Maciej Wiewiorowski - a man of action and a visionary 1918-2005